Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.
An enzyme that catalyzes the endonucleolytic cleavage of pancreatic ribonucleic acids to 3'-phosphomono- and oligonucleotides ending in cytidylic or uridylic acids with 2',3'-cyclic phosphate intermediates. EC
An enzyme catalyzing the endonucleolytic cleavage of RNA at the 3'-position of a guanylate residue. EC
A ribonuclease that specifically cleaves the RNA moiety of RNA:DNA hybrids. It has been isolated from a wide variety of prokaryotic and eukaryotic organisms as well as RETROVIRUSES.
An RNA-containing enzyme that plays an essential role in tRNA processing by catalyzing the endonucleolytic cleavage of TRANSFER RNA precursors. It removes the extra 5'-nucleotides from tRNA precursors to generate mature tRNA molecules.
A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-.
Hormones produced by the placenta include CHORIONIC GONADOTROPIN, and PLACENTAL LACTOGEN as well as steroids (ESTROGENS; PROGESTERONE), and neuropeptide hormones similar to those found in the hypothalamus (HYPOTHALAMIC HORMONES).
An endoribonuclease that is specific for double-stranded RNA. It plays a role in POST-TRANSCRIPTIONAL RNA PROCESSING of pre-RIBOSOMAL RNA and a variety of other RNA structures that contain double-stranded regions.
A 19-kDa cationic peptide found in EOSINOPHIL granules. Eosinophil-derived neurotoxin is a RIBONUCLEASE and may play a role as an endogenous antiviral agent.
A group of ribonucleotides (up to 12) in which the phosphate residues of each ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
Cytidine (dihydrogen phosphate). A cytosine nucleotide containing one phosphate group esterified to the sugar moiety in the 2', 3' or 5' position.
A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.-
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A ribonuclease activity that is a component of the HIV REVERSE TRANSCRIPTASE. It removes the RNA strand of the RNA-DNA heteroduplex produced by reverse transcription. Once the RNA moiety is removed a double stranded DNA copy of the HIV RNA can be synthesized.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
RNA that has catalytic activity. The catalytic RNA sequence folds to form a complex surface that can function as an enzyme in reactions with itself and other molecules. It may function even in the absence of protein. There are numerous examples of RNA species that are acted upon by catalytic RNA, however the scope of this enzyme class is not limited to a particular type of substrate.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The rate dynamics in chemical or physical systems.
A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.
Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
Artiodactyla is an order of mammals characterized by an even number of digits (two or four) on each foot, hooves as terminal appendages, and a specialized stomach for fermentative digestion, which includes taxonomic families such as Suidae, Cervidae, Bovidae, and Camelidae among others.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
The most abundant form of RNA. Together with proteins, it forms the ribosomes, playing a structural role and also a role in ribosomal binding of mRNA and tRNAs. Individual chains are conventionally designated by their sedimentation coefficients. In eukaryotes, four large chains exist, synthesized in the nucleolus and constituting about 50% of the ribosome. (Dorland, 28th ed)
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Polynucleotides are long, multiple-unit chains of nucleotides, the monomers that make up DNA and RNA, which carry genetic information and play crucial roles in various biological processes.
A group of 13 or more ribonucleotides in which the phosphate residues of each ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Enzymes that catalyze the hydrolysis of the internal bonds and thereby the formation of polynucleotides or oligonucleotides from ribo- or deoxyribonucleotide chains. EC 3.1.-.
A group of cytosine ribonucleotides in which the phosphate residues of each cytosine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
An essential amino acid that is required for the production of HISTAMINE.
Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Enzymes which catalyze the hydrolases of ester bonds within DNA. EC 3.1.-.
A reaction that severs one of the sugar-phosphate linkages of the phosphodiester backbone of RNA. It is catalyzed enzymatically, chemically, or by radiation. Cleavage may be exonucleolytic, or endonucleolytic.
An enzyme of the transferase class that catalyzes the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, IDP, GDP, UDP, and CDP can act as donors in the latter case. (From Dorland, 27th ed) EC
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
An intracellular ribonucleolytic protein complex that participates in POSTRANSCRIPTIONAL RNA PROCESSING and RNA DEGRADATION.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Uracil nucleotides are chemical compounds that consist of a uracil base, a sugar molecule called ribose, and one or more phosphate groups, which play crucial roles in DNA replication, repair, and gene expression as well as in RNA synthesis.
Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
The process of cleaving a chemical compound by the addition of a molecule of water.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Proteins found in EOSINOPHIL granules. They are primarily basic proteins that play a role in host defense and the proinflammatory actions of activated eosinophils.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The sum of the weight of all the atoms in a molecule.
Cytosine nucleotides are organic compounds that consist of a nitrogenous base (cytosine), a pentose sugar (ribose in RNA or deoxyribose in DNA), and at least one phosphate group, playing crucial roles in genetic information storage, transmission, and expression within nucleic acids.
RNA transcripts of the DNA that are in some unfinished stage of post-transcriptional processing (RNA PROCESSING, POST-TRANSCRIPTIONAL) required for function. RNA precursors may undergo several steps of RNA SPLICING during which the phosphodiester bonds at exon-intron boundaries are cleaved and the introns are excised. Consequently a new bond is formed between the ends of the exons. Resulting mature RNAs can then be used; for example, mature mRNA (RNA, MESSENGER) is used as a template for protein production.
Slow-moving exclusively arboreal mammals that inhabit the tropical forests of South and Central America.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An order of New World mammals characterized by the absence of incisors and canines from among their teeth, and comprising the ARMADILLOS, the SLOTHS, and the anteaters. The order is distinguished from all others by what are known as xenarthrous vertebrae (xenos, strange; arthron, joint): there are secondary, and sometimes even more, articulations between the vertebrae of the lumbar series. The order was formerly called Edentata. (From Random House Unabridged Dictionary, 2d ed; Walker's Mammals of the World, 5th ed, vol. I, p515)
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
Polymers made up of a few (2-20) nucleotides. In molecular genetics, they refer to a short sequence synthesized to match a region where a mutation is known to occur, and then used as a probe (OLIGONUCLEOTIDE PROBES). (Dorland, 28th ed)
Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
Proteins obtained from ESCHERICHIA COLI.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
Uridine is a nucleoside, specifically a derivative of pyrimidine, that is composed of a uracil molecule joined to a ribose sugar molecule through a β-N1 glycosidic bond, and has significant roles in RNA synthesis, energy transfer, and cell signaling.
Post-transcriptional biological modification of messenger, transfer, or ribosomal RNAs or their precursors. It includes cleavage, methylation, thiolation, isopentenylation, pseudouridine formation, conformational changes, and association with ribosomal protein.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis.
A group of compounds which consist of a nucleotide molecule to which an additional nucleoside is attached through the phosphate molecule(s). The nucleotide can contain any number of phosphates.
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992)
One of several basic proteins released from EOSINOPHIL cytoplasmic granules. Eosinophil cationic protein is a 21-kDa cytotoxic peptide with a pI of 10.9. Although eosinophil cationic protein is considered a member of the RNAse A superfamily of proteins, it has only limited RNAse activity.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Disruption of the secondary structure of nucleic acids by heat, extreme pH or chemical treatment. Double strand DNA is "melted" by dissociation of the non-covalent hydrogen bonds and hydrophobic interactions. Denatured DNA appears to be a single-stranded flexible structure. The effects of denaturation on RNA are similar though less pronounced and largely reversible.
Proteins prepared by recombinant DNA technology.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An enzyme that synthesizes DNA on an RNA template. It is encoded by the pol gene of retroviruses and by certain retrovirus-like elements. EC
RNA consisting of two strands as opposed to the more prevalent single-stranded RNA. Most of the double-stranded segments are formed from transcription of DNA by intramolecular base-pairing of inverted complementary sequences separated by a single-stranded loop. Some double-stranded segments of RNA are normal in all organisms.
A group of uridine ribonucleotides in which the phosphate residues of each uridine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
An actinomycete from which the antibiotic CHLORTETRACYCLINE is obtained.
The extent to which an RNA molecule retains its structural integrity and resists degradation by RNASE, and base-catalyzed HYDROLYSIS, under changing in vivo or in vitro conditions.
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.
Complexes of RNA-binding proteins with ribonucleic acids (RNA).
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC
A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Ribonucleic acid that makes up the genetic material of viruses.
A genus of zygomycetous fungi of the family Mucoraceae, order MUCORALES, a common saprophyte and facultative parasite of mature fruits and vegetables. It may cause cerebral mycoses in diabetes and cutaneous infection in severely burned patients.
A transfer RNA which is specific for carrying tyrosine to sites on the ribosomes in preparation for protein synthesis.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
A genus of mitosporic fungi containing about 100 species and eleven different teleomorphs in the family Trichocomaceae.
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
Tritium is an isotope of hydrogen (specifically, hydrogen-3) that contains one proton and two neutrons in its nucleus, making it radioactive with a half-life of about 12.3 years, and is used in various applications including nuclear research, illumination, and dating techniques due to its low energy beta decay.
A group of inosine ribonucleotides in which the phosphate residues of each inosine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
5'-Uridylic acid. A uracil nucleotide containing one phosphate group esterified to the sugar moiety in the 2', 3' or 5' position.
A family of iminourea derivatives. The parent compound has been isolated from mushrooms, corn germ, rice hulls, mussels, earthworms, and turnip juice. Derivatives may have antiviral and antifungal properties.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Techniques for measuring specific nucleic acid interaction with another nucleic acid or with a protein by digestion of the non-interacting nucleic acid by various nucleases. After all non-interacting regions are eliminated by nuclease digestion, the protected nucleic acid that remains is analyzed. DNA FOOTPRINTING utilizes this technique to analyze the DNA contact sites of DNA-BINDING PROTEINS.
A type of ion exchange chromatography using diethylaminoethyl cellulose (DEAE-CELLULOSE) as a positively charged resin. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Stable phosphorus atoms that have the same atomic number as the element phosphorus, but differ in atomic weight. P-31 is a stable phosphorus isotope.
A group of adenine ribonucleotides in which the phosphate residues of each adenine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An analytical technique for resolution of a chemical mixture into its component compounds. Compounds are separated on an adsorbent paper (stationary phase) by their varied degree of solubility/mobility in the eluting solvent (mobile phase).
The thick, yellowish-white, viscid fluid secretion of male reproductive organs discharged upon ejaculation. In addition to reproductive organ secretions, it contains SPERMATOZOA and their nutrient plasma.
RNA, usually prepared by transcription from cloned DNA, which complements a specific mRNA or DNA and is generally used for studies of virus genes, distribution of specific RNA in tissues and cells, integration of viral DNA into genomes, transcription, etc. Whereas DNA PROBES are preferred for use at a more macroscopic level for detection of the presence of DNA/RNA from specific species or subspecies, RNA probes are preferred for genetic studies. Conventional labels for the RNA probe include radioisotope labels 32P and 125I and the chemical label biotin. RNA probes may be further divided by category into plus-sense RNA probes, minus-sense RNA probes, and antisense RNA probes.
Guanine nucleotides are cyclic or linear molecules that consist of a guanine base, a pentose sugar (ribose in the cyclic form, deoxyribose in the linear form), and one or more phosphate groups, playing crucial roles in signal transduction, protein synthesis, and regulation of enzymatic activities.
Nucleotides in which the purine or pyrimidine base is combined with ribose. (Dorland, 28th ed)
A phylum of fungi that produce their sexual spores (basidiospores) on the outside of the basidium. It includes forms commonly known as mushrooms, boletes, puffballs, earthstars, stinkhorns, bird's-nest fungi, jelly fungi, bracket or shelf fungi, and rust and smut fungi.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Topical antiseptic used mainly in wound dressings.
An electrochemical process in which macromolecules or colloidal particles with a net electric charge migrate in a solution under the influence of an electric current.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
The monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th ed)
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.
A reverse transcriptase encoded by the POL GENE of HIV. It is a heterodimer of 66 kDa and 51 kDa subunits that are derived from a common precursor protein. The heterodimer also includes an RNAse H activity (RIBONUCLEASE H, HUMAN IMMUNODEFICIENCY VIRUS) that plays an essential role the viral replication process.
A double-stranded polyribonucleotide comprising polyadenylic and polyuridylic acids.

Gene silencing: plants and viruses fight it out. (1/4689)

Plants can become 'immune' to attack by viruses by degrading specific viral RNA, but some plant viruses have evolved the general capacity to suppress this resistance mechanism.  (+info)

Structural basis for the specificity of the initiation of HIV-1 reverse transcription. (2/4689)

Initiation of human immunodeficiency virus type 1 (HIV-1) reverse transcription requires specific recognition of the viral genome, tRNA3Lys, which acts as primer, and reverse transcriptase (RT). The specificity of this ternary complex is mediated by intricate interactions between HIV-1 RNA and tRNA3Lys, but remains poorly understood at the three-dimensional level. We used chemical probing to gain insight into the three-dimensional structure of the viral RNA-tRNA3Lys complex, and enzymatic footprinting to delineate regions interacting with RT. These and previous experimental data were used to derive a three-dimensional model of the initiation complex. The viral RNA and tRNA3Lys form a compact structure in which the two RNAs fold into distinct structural domains. The extended interactions between these molecules are not directly recognized by RT. Rather, they favor RT binding by preventing steric clashes between the nucleic acids and the polymerase and inducing a viral RNA-tRNA3Lys conformation which fits perfectly into the nucleic acid binding cleft of RT. Recognition of the 3' end of tRNA3Lys and of the first template nucleotides by RT is favored by a kink in the template strand promoted by the short junctions present in the previously established secondary structure.  (+info)

Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay. (3/4689)

We have identified a cellular target for proteasomal endonuclease activity. Thus, 20 S proteasomes interact with the 3'-untranslated region of certain cytoplasmic mRNAs in vivo, and 20 S proteasomes isolated from Friend leukemia virus-infected mouse spleen cells were found to be associated with a mRNA fragment showing great homology to the 3'-untranslated region of tumor necrosis factor-beta mRNA that contains AUUUA sequences. We furthermore demonstrate that 20 S proteasomes destabilize oligoribonucleotides corresponding to the 3'-untranslated region of tumor necrosis factor-alpha, creating a specific cleavage pattern. The cleavage reaction is accelerated with increasing number of AUUUA motifs, and major cleavage sites are localized at the 5' side of the A residues. These results strongly suggest that 20 S proteasomes could be involved in the destabilization of cytokine mRNAs such as tumor necrosis factor mRNAs and other short-lived mRNAs containing AUUUA sequences.  (+info)

Characterization of nuclear structures containing superhelical DNA. (4/4689)

Structures resembling nuclei but depleted of protein may be released by gently lysing cells in solutions containing non-ionic detergents and high concentrations of salt. These nucleoids sediment in gradients containing intercalating agents in a manner characteristic of DNA that is intact, supercoiled and circular. The concentration of salt present during isolation of human nucleoids affects their protein content. When made in I-95 M NaCl they lack histones and most of the proteins characteristic of chromatin; in 1-0 M NaCl they contain variable amounts of histones. The effects of various treatments on nucleoid integrity were investigated.  (+info)

Purification of gibberellic acid-induced lysosomes from wheat aleurone cells. (5/4689)

Using isopycnic density gradient centrifugation, lysosomes were concentrated in a single region of a sucrose-Ficoll gradient (p = 1-10 g cm-3), well separated from most other cell organelles. Gibberellic acid-induced lysosomes were found to be rich in alpha-amylase and protease but not ribonuclease. The lysosomal band also contained a majority of the NADH2-cytochrome c reductase, a marker enzyme for endoplasmic reticulum, found in the gradient. Examination of electron micrographs revealed that a purified band of lyosomes contained at least 3 vesicle types, ranging in size from 0-1 to 0-5 mum. The significance of these findings to proposed mechanisms of action of gibberellic acid is discussed.  (+info)

Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene. (6/4689)

We have previously shown (K. Kas et al, Nat. Genet., 15: 170-174, 1997) that the developmentally regulated zinc finger gene pleomorphic adenoma gene 1 (PLAG1) is the target gene in 8q12 in pleomorphic adenomas of the salivary glands with t(3;8)(p21;q12) translocations. The t(3;8) results in promoter swapping between PLAG1 and the constitutively expressed gene for beta-catenin (CTNNB1), leading to activation of PLAG1 expression and reduced expression of CTNNB1. Here we have studied the expression of PLAG1 by Northern blot analysis in 47 primary benign and malignant human tumors with or without cytogenetic abnormalities of 8q12. Overexpression of PLAG1 was found in 23 tumors (49%). Thirteen of 17 pleomorphic adenomas with a normal karyotype and 5 of 10 with 12q13-15 abnormalities overexpressed PLAG1, which demonstrates that PLAG1 activation is a frequent event in adenomas irrespective of karyotype. In contrast, PLAG1 was overexpressed in only 2 of 11 malignant salivary gland tumors analyzed, which suggests that, at least in salivary gland tumors, PLAG1 activation preferentially occurs in benign tumors. PLAG1 over-expression was also found in three of nine mesenchymal tumors, i.e., in two uterine leiomyomas and one leiomyosarcoma. RNase protection, rapid amplification of 5'-cDNA ends (5'-RACE), and reverse transcription-PCR analyses of five adenomas with a normal karyotype revealed fusion transcripts in three tumors. Nucleotide sequence analysis of these showed that they contained fusions between PLAG1 and CTNNB1 (one case) or PLAG1 and a novel fusion partner gene, i.e., the gene encoding the transcription elongation factor SII (two cases). The fusions occurred in the 5' noncoding region of PLAG1, leading to exchange of regulatory control elements and, as a consequence, activation of PLAG1 gene expression. Because all of the cases had grossly normal karyotypes, the rearrangements must result from cryptic rearrangements. The results suggest that in addition to chromosomal translocations and cryptic rearrangements, PLAG1 may also be activated by mutations or indirect mechanisms. Our findings establish a conserved mechanism of PLAG1 activation in salivary gland tumors with and without 8q12 aberrations, which indicates that such activation is a frequent event in these tumors.  (+info)

Simplified methods for pKa and acid pH-dependent stability estimation in proteins: removing dielectric and counterion boundaries. (7/4689)

Much computational research aimed at understanding ionizable group interactions in proteins has focused on numerical solutions of the Poisson-Boltzmann (PB) equation, incorporating protein exclusion zones for solvent and counterions in a continuum model. Poor agreement with measured pKas and pH-dependent stabilities for a (protein, solvent) relative dielectric boundary of (4,80) has lead to the adoption of an intermediate (20,80) boundary. It is now shown that a simple Debye-Huckel (DH) calculation, removing both the low dielectric and counterion exclusion regions associated with protein, is equally effective in general pKa calculations. However, a broad-based discrepancy to measured pH-dependent stabilities is maintained in the absence of ionizable group interactions in the unfolded state. A simple model is introduced for these interactions, with a significantly improved match to experiment that suggests a potential utility in predicting and analyzing the acid pH-dependence of protein stability. The methods are applied to the relative pH-dependent stabilities of the pore-forming domains of colicins A and N. The results relate generally to the well-known preponderance of surface ionizable groups with solvent-mediated interactions. Although numerical PB solutions do not currently have a significant advantage for overall pKa estimations, development based on consideration of microscopic solvation energetics in tandem with the continuum model could combine the large deltapKas of a subset of ionizable groups with the overall robustness of the DH model.  (+info)

Variants of ribonuclease inhibitor that resist oxidation. (8/4689)

Human ribonuclease inhibitor (hRI) is a cytosolic protein that protects cells from the adventitious invasion of pancreatic-type ribonucleases. hRI has 32 cysteine residues. The oxidation of these cysteine residues to form disulfide bonds is a rapid, cooperative process that inactivates hRI. The most proximal cysteine residues in native hRI are two pairs that are adjacent in sequence: Cys94 and Cys95, and Cys328 and Cys329. A cystine formed from such adjacent cysteine residues would likely contain a perturbing cis peptide bond within its eight-membered ring, which would disrupt the structure of hRI and could facilitate further oxidation. We find that replacing Cys328 and Cys329 with alanine residues has little effect on the affinity of hRI for bovine pancreatic ribonuclease A (RNase A), but increases its resistance to oxidation by 10- to 15-fold. Similar effects are observed for the single variants, C328A hRI and C329A hRI, suggesting that oxidation resistance arises from the inability to form a Cys328-Cys329 disulfide bond. Replacing Cys94 and Cys95 with alanine residues increases oxidation resistance to a lesser extent, and decreases the affinity of hRI for RNase A. The C328A, C329A, and C328A/C329A variants are likely to be more useful than wild-type hRI for inhibiting pancreatic-type ribonucleases in vitro and in vivo. We conclude that replacing adjacent cysteine residues can confer oxidation resistance in a protein.  (+info)

Ribonucleases (RNases) are a group of enzymes that catalyze the degradation of ribonucleic acid (RNA) molecules by hydrolyzing the phosphodiester bonds. These enzymes play crucial roles in various biological processes, such as RNA processing, turnover, and quality control. They can be classified into several types based on their specificities, mechanisms, and cellular localizations.

Some common classes of ribonucleases include:

1. Endoribonucleases: These enzymes cleave RNA internally, at specific sequences or structural motifs. Examples include RNase A, which targets single-stranded RNA; RNase III, which cuts double-stranded RNA at specific stem-loop structures; and RNase T1, which recognizes and cuts unpaired guanosine residues in RNA molecules.
2. Exoribonucleases: These enzymes remove nucleotides from the ends of RNA molecules. They can be further divided into 5'-3' exoribonucleases, which degrade RNA starting from the 5' end, and 3'-5' exoribonucleases, which start at the 3' end. Examples include Xrn1, a 5'-3' exoribonuclease involved in mRNA decay; and Dis3/RRP6, a 3'-5' exoribonuclease that participates in ribosomal RNA processing and degradation.
3. Specific ribonucleases: These enzymes target specific RNA molecules or regions with high precision. For example, RNase P is responsible for cleaving the 5' leader sequence of precursor tRNAs (pre-tRNAs) during their maturation; and RNase MRP is involved in the processing of ribosomal RNA and mitochondrial RNA molecules.

Dysregulation or mutations in ribonucleases have been implicated in various human diseases, such as neurological disorders, cancer, and viral infections. Therefore, understanding their functions and mechanisms is crucial for developing novel therapeutic strategies.

Ribonuclease, pancreatic (also known as RNase pancreatica or RNase 1) is a type of enzyme that belongs to the ribonuclease family. This enzyme is produced in the pancreas and is released into the small intestine during digestion. Its primary function is to help break down RNA (ribonucleic acid), which is present in ingested food, into smaller components called nucleotides. This process aids in the absorption of nutrients from the gastrointestinal tract.

Ribonuclease, pancreatic is a single-chain protein with a molecular weight of approximately 13.7 kDa. It has a specific affinity for single-stranded RNA and exhibits endonucleolytic activity, meaning it can cut the RNA chain at various internal points. This enzyme plays an essential role in the digestion and metabolism of RNA in the human body.

Ribonuclease T1 is a type of enzyme that belongs to the ribonuclease family. Its primary function is to cleave or cut single-stranded RNA molecules at specific sites, particularly after guanine residues. This enzyme is produced by various organisms, including fungi and humans, and it plays a crucial role in the regulation of RNA metabolism and function.

In particular, Ribonuclease T1 from Aspergillus oryzae is widely used in biochemical and molecular biology research due to its specificity for single-stranded RNA and its ability to cleave RNA molecules into small fragments. This enzyme has been extensively used in techniques such as RNase protection assays, structure probing, and mapping of RNA secondary structures.

Ribonuclease H (RNase H) is an enzyme that specifically degrades the RNA portion of an RNA-DNA hybrid. It cleaves the phosphodiester bond between the ribose sugar and the phosphate group in the RNA strand, leaving the DNA strand intact. This enzyme plays a crucial role in several cellular processes, including DNA replication, repair, and transcription.

There are two main types of RNase H: type 1 and type 2. Type 1 RNase H is found in both prokaryotic and eukaryotic cells, while type 2 RNase H is primarily found in eukaryotes. The primary function of RNase H is to remove RNA primers that are synthesized during DNA replication. These RNA primers are replaced with DNA nucleotides by another enzyme called polymerase δ, leaving behind a gap in the DNA strand. RNase H then cleaves the RNA-DNA hybrid, allowing for the repair of the gap and the completion of DNA replication.

RNase H has also been implicated in the regulation of gene expression, as it can degrade RNA-DNA hybrids formed during transcription. This process, known as transcription-coupled RNA decay, helps to prevent the accumulation of aberrant RNA molecules and ensures proper gene expression.

In addition to its cellular functions, RNase H has been studied for its potential therapeutic applications. For example, inhibitors of RNase H have been shown to have antiviral activity against HIV-1, as they prevent the degradation of viral RNA during reverse transcription. On the other hand, activators of RNase H have been explored as a means to enhance the efficiency of RNA interference (RNAi) therapies by promoting the degradation of target RNA molecules.

Ribonuclease P (RNase P) is an endonuclease enzyme complex that is found in all three domains of life: archaea, bacteria, and eukaryotes. Its primary function is to process precursor transfer RNA (tRNA) molecules by cleaving the 5' leader sequence to generate mature tRNAs.

RNase P is unique because it consists of both a protein component and an RNA subunit, known as the RNA moiety or RNA catalytic subunit. In bacteria and archaea, the RNA subunit is primarily responsible for the enzymatic activity, while in eukaryotes, the protein component plays a more significant role.

RNase P's function in tRNA processing is essential for protein synthesis, as mature tRNAs are necessary for decoding messenger RNA (mRNA) sequences and translating them into proteins during translation. Dysregulation or mutations in RNase P can lead to various human diseases, including mitochondrial disorders, neurodevelopmental abnormalities, and cancer.

Endoribonucleases are enzymes that cleave RNA molecules internally, meaning they cut the phosphodiester bond between nucleotides within the RNA chain. These enzymes play crucial roles in various cellular processes, such as RNA processing, degradation, and quality control. Different endoribonucleases recognize specific sequences or structural features in RNA substrates, allowing them to target particular regions for cleavage. Some well-known examples of endoribonucleases include RNase III, RNase T1, and RNase A, each with distinct substrate preferences and functions.

Placental hormones are a type of hormones that are produced by the placenta, an organ that develops in the uterus during pregnancy. These hormones play a crucial role in maintaining and supporting a healthy pregnancy. Some of the key placental hormones include:

1. Human Chorionic Gonadotropin (hCG): This hormone is produced after implantation and is detected in the urine or blood to confirm pregnancy. It maintains the corpus luteum, which produces progesterone during early pregnancy.
2. Progesterone: This hormone is critical for preparing the uterus for pregnancy and maintaining the pregnancy. It suppresses maternal immune response to prevent rejection of the developing embryo/fetus.
3. Estrogen: This hormone plays a vital role in the growth and development of the fetal brain, as well as promoting the growth of the uterus and mammary glands during pregnancy.
4. Human Placental Lactogen (hPL): This hormone stimulates maternal metabolism to provide nutrients for the developing fetus and helps prepare the breasts for lactation.
5. Relaxin: This hormone relaxes the pelvic ligaments and softens and widens the cervix in preparation for childbirth.

These hormones work together to support fetal growth, maintain pregnancy, and prepare the mother's body for childbirth and lactation.

Ribonuclease III, also known as RNase III or double-stranded RNA specific endonuclease, is an enzyme that belongs to the endoribonuclease family. This enzyme is responsible for cleaving double-stranded RNA (dsRNA) molecules into smaller fragments of approximately 20-25 base pairs in length. The resulting fragments are called small interfering RNAs (siRNAs), which play a crucial role in the regulation of gene expression through a process known as RNA interference (RNAi).

Ribonuclease III functions by recognizing and binding to specific stem-loop structures within dsRNA molecules, followed by cleaving both strands at precise locations. This enzyme is highly conserved across various species, including bacteria, yeast, plants, and animals, indicating its fundamental role in cellular processes. In addition to its involvement in RNAi, ribonuclease III has been implicated in the maturation of other non-coding RNAs, such as microRNAs (miRNAs) and transfer RNAs (tRNAs).

Eosinophil-Derived Neurotoxin (EDN) is a protein that is released from the granules of eosinophils, which are a type of white blood cell involved in the immune response. EDN has both neurotoxic and ribonucleolytic activities, meaning it can damage nerve cells and also degrade RNA. It is thought to play a role in the pathogenesis of certain diseases such as asthma and some forms of inflammatory bowel disease. EDN is also known as eosinophil cationic protein or ECP.

Oligoribonucleotides are short, synthetic chains of ribonucleotides, which are the building blocks of RNA (ribonucleic acid). These chains typically contain fewer than 20 ribonucleotide units, and can be composed of all four types of nucleotides found in RNA: adenine (A), uracil (U), guanine (G), and cytosine (C). They are often used in research for various purposes, such as studying RNA function, regulating gene expression, or serving as potential therapeutic agents.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

The pancreas is a glandular organ located in the abdomen, posterior to the stomach. It has both exocrine and endocrine functions. The exocrine portion of the pancreas consists of acinar cells that produce and secrete digestive enzymes into the duodenum via the pancreatic duct. These enzymes help in the breakdown of proteins, carbohydrates, and fats in food.

The endocrine portion of the pancreas consists of clusters of cells called islets of Langerhans, which include alpha, beta, delta, and F cells. These cells produce and secrete hormones directly into the bloodstream, including insulin, glucagon, somatostatin, and pancreatic polypeptide. Insulin and glucagon are critical regulators of blood sugar levels, with insulin promoting glucose uptake and storage in tissues and glucagon stimulating glycogenolysis and gluconeogenesis to raise blood glucose when it is low.

Cytidine monophosphate (CMP) is a nucleotide that consists of a cytosine molecule attached to a ribose sugar molecule, which in turn is linked to a phosphate group. It is one of the four basic building blocks of RNA (ribonucleic acid) along with adenosine monophosphate (AMP), guanosine monophosphate (GMP), and uridine monophosphate (UMP). CMP plays a critical role in various biochemical reactions within the body, including protein synthesis and energy metabolism.

Exoribonucleases are a type of enzyme that degrade RNA molecules in a process called exoribonucleolysis. They remove nucleotides from the end of an RNA strand, working their way inwards towards the middle of the strand. Exoribonucleases can be specific for single-stranded or double-stranded RNA, and some can discriminate between different types of RNA molecules based on sequence or structure. They play important roles in various cellular processes, including RNA degradation, quality control, and maturation.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Ribonuclease H, Human Immunodeficiency Virus (HIV RNase H) is an enzyme that is encoded by the pol gene of the human immunodeficiency virus (HIV). This enzyme plays a crucial role in the replication of the HIV genome.

The primary function of HIV RNase H is to degrade the RNA portion of the RNA-DNA hybrid that is formed during reverse transcription, which is the process by which HIV converts its RNA genome into DNA. By removing the RNA component of this hybrid, HIV RNase H allows for the integration of the viral DNA into the host cell's genome, thereby facilitating viral replication.

HIV RNase H is a potential target for antiretroviral therapy (ART) as inhibiting its activity can prevent the virus from replicating and thus slow down or stop the progression of HIV infection. However, there are currently no approved drugs that specifically target HIV RNase H, and further research is needed to develop effective inhibitors of this enzyme.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

RNA (Ribonucleic Acid) is a single-stranded, linear polymer of ribonucleotides. It is a nucleic acid present in the cells of all living organisms and some viruses. RNAs play crucial roles in various biological processes such as protein synthesis, gene regulation, and cellular signaling. There are several types of RNA including messenger RNA (mRNA), ribosomal RNA (rRNA), transfer RNA (tRNA), small nuclear RNA (snRNA), microRNA (miRNA), and long non-coding RNA (lncRNA). These RNAs differ in their structure, function, and location within the cell.

A catalytic RNA, often referred to as a ribozyme, is a type of RNA molecule that has the ability to act as an enzyme and catalyze chemical reactions. These RNA molecules contain specific sequences and structures that allow them to bind to other molecules and accelerate chemical reactions without being consumed in the process.

Ribozymes play important roles in various biological processes, such as RNA splicing, translation regulation, and gene expression. One of the most well-known ribozymes is the self-splicing intron found in certain RNA molecules, which can excise itself from the host RNA and then ligase the flanking exons together.

The discovery of catalytic RNAs challenged the central dogma of molecular biology, which held that proteins were solely responsible for carrying out biological catalysis. The finding that RNA could also function as an enzyme opened up new avenues of research and expanded our understanding of the complexity and versatility of biological systems.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Guanosine monophosphate (GMP) is a nucleotide that is a fundamental unit of genetic material in DNA and RNA. It consists of a guanine base, a pentose sugar (ribose in the case of RNA, deoxyribose in DNA), and one phosphate group. GMP plays crucial roles in various biochemical reactions within cells, including energy transfer and signal transduction pathways. Additionally, it is involved in the synthesis of important molecules like nucleic acids, neurotransmitters, and hormones.

Bacterial RNA refers to the genetic material present in bacteria that is composed of ribonucleic acid (RNA). Unlike higher organisms, bacteria contain a single circular chromosome made up of DNA, along with smaller circular pieces of DNA called plasmids. These bacterial genetic materials contain the information necessary for the growth and reproduction of the organism.

Bacterial RNA can be divided into three main categories: messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA). mRNA carries genetic information copied from DNA, which is then translated into proteins by the rRNA and tRNA molecules. rRNA is a structural component of the ribosome, where protein synthesis occurs, while tRNA acts as an adapter that brings amino acids to the ribosome during protein synthesis.

Bacterial RNA plays a crucial role in various cellular processes, including gene expression, protein synthesis, and regulation of metabolic pathways. Understanding the structure and function of bacterial RNA is essential for developing new antibiotics and other therapeutic strategies to combat bacterial infections.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Nucleic acid conformation refers to the three-dimensional structure that nucleic acids (DNA and RNA) adopt as a result of the bonding patterns between the atoms within the molecule. The primary structure of nucleic acids is determined by the sequence of nucleotides, while the conformation is influenced by factors such as the sugar-phosphate backbone, base stacking, and hydrogen bonding.

Two common conformations of DNA are the B-form and the A-form. The B-form is a right-handed helix with a diameter of about 20 Å and a pitch of 34 Å, while the A-form has a smaller diameter (about 18 Å) and a shorter pitch (about 25 Å). RNA typically adopts an A-form conformation.

The conformation of nucleic acids can have significant implications for their function, as it can affect their ability to interact with other molecules such as proteins or drugs. Understanding the conformational properties of nucleic acids is therefore an important area of research in molecular biology and medicine.

Artiodactyla is an order of mammals that includes even-toed ungulates, or hooved animals, with an odd number of toes. This group includes animals such as pigs, peccaries, hippos, camels, deer, giraffes, antelopes, and ruminants like cattle, sheep, and goats. The primary identifying feature of Artiodactyls is the presence of a pair of weight-bearing toes located in the middle of the foot, with the other toes being either reduced or absent. This arrangement provides stability and adaptability for these animals to thrive in various habitats worldwide.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Protein denaturation is a process in which the native structure of a protein is altered, leading to loss of its biological activity. This can be caused by various factors such as changes in temperature, pH, or exposure to chemicals or radiation. The three-dimensional shape of a protein is crucial for its function, and denaturation causes the protein to lose this shape, resulting in impaired or complete loss of function. Denaturation is often irreversible and can lead to the aggregation of proteins, which can have negative effects on cellular function and can contribute to diseases such as Alzheimer's and Parkinson's.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. In protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

Each tRNA molecule has a distinct structure, consisting of approximately 70-90 nucleotides arranged in a cloverleaf shape with several loops and stems. The most important feature of a tRNA is its anticodon, a sequence of three nucleotides located in one of the loops. This anticodon base-pairs with a complementary codon on the mRNA during translation, ensuring that the correct amino acid is added to the growing polypeptide chain.

Before tRNAs can participate in protein synthesis, they must be charged with their specific amino acids through an enzymatic process involving aminoacyl-tRNA synthetases. These enzymes recognize and bind to both the tRNA and its corresponding amino acid, forming a covalent bond between them. Once charged, the aminoacyl-tRNA complex is ready to engage in translation and contribute to protein formation.

In summary, transfer RNA (tRNA) is a small RNA molecule that facilitates protein synthesis by translating genetic information from messenger RNA into specific amino acids, ultimately leading to the creation of functional proteins within cells.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Ribosomal RNA (rRNA) is a type of RNA molecule that is a key component of ribosomes, which are the cellular structures where protein synthesis occurs in cells. In ribosomes, rRNA plays a crucial role in the process of translation, where genetic information from messenger RNA (mRNA) is translated into proteins.

Ribosomal RNA is synthesized in the nucleus and then transported to the cytoplasm, where it assembles with ribosomal proteins to form ribosomes. Within the ribosome, rRNA provides a structural framework for the assembly of the ribosome and also plays an active role in catalyzing the formation of peptide bonds between amino acids during protein synthesis.

There are several different types of rRNA molecules, including 5S, 5.8S, 18S, and 28S rRNA, which vary in size and function. These rRNA molecules are highly conserved across different species, indicating their essential role in protein synthesis and cellular function.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Polynucleotides are long, chain-like molecules composed of repeating units called nucleotides. Each nucleotide contains a sugar molecule (deoxyribose in DNA or ribose in RNA), a phosphate group, and a nitrogenous base (adenine, guanine, cytosine, thymine in DNA or adenine, guanine, uracil, cytosine in RNA). In DNA, the nucleotides are joined together by phosphodiester bonds between the sugar of one nucleotide and the phosphate group of the next, creating a double helix structure. In RNA, the nucleotides are also joined by phosphodiester bonds but form a single strand. Polynucleotides play crucial roles in storing and transmitting genetic information within cells.

Polyribonucleotides are long, chain-like molecules composed of multiple ribonucleotide monomers. Ribonucleotides themselves consist of a ribose sugar, a phosphate group, and one of the four nitrogenous bases: adenine (A), uracil (U), guanine (G), or cytosine (C). In polyribonucleotides, these ribonucleotide monomers are linked together by ester bonds between the phosphate group of one monomer and the ribose sugar of another.

These molecules play crucial roles in various biological processes, such as encoding genetic information, regulating gene expression, catalyzing chemical reactions, and serving as structural components within cells. Some examples of polyribonucleotides include messenger RNA (mRNA), ribosomal RNA (rRNA), transfer RNA (tRNA), and small nuclear RNA (snRNA).

In a medical context, polyribonucleotides may be used in therapeutic applications, such as gene therapy or vaccines. For instance, synthetic mRNAs can be designed to encode specific proteins, which can then be introduced into cells to stimulate the production of those proteins for various purposes, including immunization against infectious diseases or cancer treatment.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Endonucleases are enzymes that cleave, or cut, phosphodiester bonds within a polynucleotide chain, specifically within the same molecule of DNA or RNA. They can be found in all living organisms and play crucial roles in various biological processes, such as DNA replication, repair, and recombination.

Endonucleases can recognize specific nucleotide sequences (sequence-specific endonucleases) or have no sequence preference (non-specific endonucleases). Some endonucleases generate sticky ends, overhangs of single-stranded DNA after cleavage, while others produce blunt ends without any overhang.

These enzymes are widely used in molecular biology techniques, such as restriction digestion, cloning, and genome editing (e.g., CRISPR-Cas9 system). Restriction endonucleases recognize specific DNA sequences called restriction sites and cleave the phosphodiester bonds at or near these sites, generating defined fragment sizes that can be separated by agarose gel electrophoresis. This property is essential for various applications in genetic engineering and biotechnology.

I'm sorry for any confusion, but "Poly C" is not a widely recognized medical term or abbreviation in the field of medicine or biology. It might be a typographical error or a shorthand notation used in a specific context. If you could provide more context or clarify what you mean by "Poly C," I would be happy to help further.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Histidine is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H9N3O2. Histidine plays a crucial role in several physiological processes, including:

1. Protein synthesis: As an essential amino acid, histidine is required for the production of proteins, which are vital components of various tissues and organs in the body.

2. Hemoglobin synthesis: Histidine is a key component of hemoglobin, the protein in red blood cells responsible for carrying oxygen throughout the body. The imidazole side chain of histidine acts as a proton acceptor/donor, facilitating the release and uptake of oxygen by hemoglobin.

3. Acid-base balance: Histidine is involved in maintaining acid-base homeostasis through its role in the biosynthesis of histamine, which is a critical mediator of inflammatory responses and allergies. The decarboxylation of histidine results in the formation of histamine, which can increase vascular permeability and modulate immune responses.

4. Metal ion binding: Histidine has a high affinity for metal ions such as zinc, copper, and iron. This property allows histidine to participate in various enzymatic reactions and maintain the structural integrity of proteins.

5. Antioxidant defense: Histidine-containing dipeptides, like carnosine and anserine, have been shown to exhibit antioxidant properties by scavenging reactive oxygen species (ROS) and chelating metal ions. These compounds may contribute to the protection of proteins and DNA from oxidative damage.

Dietary sources of histidine include meat, poultry, fish, dairy products, and wheat germ. Histidine deficiency is rare but can lead to growth retardation, anemia, and impaired immune function.

Centrifugation, Density Gradient is a medical laboratory technique used to separate and purify different components of a mixture based on their size, density, and shape. This method involves the use of a centrifuge and a density gradient medium, such as sucrose or cesium chloride, to create a stable density gradient within a column or tube.

The sample is carefully layered onto the top of the gradient and then subjected to high-speed centrifugation. During centrifugation, the particles in the sample move through the gradient based on their size, density, and shape, with heavier particles migrating faster and further than lighter ones. This results in the separation of different components of the mixture into distinct bands or zones within the gradient.

This technique is commonly used to purify and concentrate various types of biological materials, such as viruses, organelles, ribosomes, and subcellular fractions, from complex mixtures. It allows for the isolation of pure and intact particles, which can then be collected and analyzed for further study or use in downstream applications.

In summary, Centrifugation, Density Gradient is a medical laboratory technique used to separate and purify different components of a mixture based on their size, density, and shape using a centrifuge and a density gradient medium.

Deoxyribonucleases (DNases) are a group of enzymes that cleave, or cut, the phosphodiester bonds in the backbone of deoxyribonucleic acid (DNA) molecules. DNases are classified based on their mechanism of action into two main categories: double-stranded DNases and single-stranded DNases.

Double-stranded DNases cleave both strands of the DNA duplex, while single-stranded DNases cleave only one strand. These enzymes play important roles in various biological processes, such as DNA replication, repair, recombination, and degradation. They are also used in research and clinical settings for applications such as DNA fragmentation analysis, DNA sequencing, and treatment of cystic fibrosis.

It's worth noting that there are many different types of DNases with varying specificities and activities, and the medical definition may vary depending on the context.

RNA cleavage is a biological process in which RNA molecules are cut or split into smaller fragments by enzymes known as ribonucleases (RNases). This process can occur co-transcriptionally, during splicing, or as a means of regulation of RNA stability and function. Cleavage sites are often defined by specific sequences or structures within the RNA molecule. The cleavage products may have various fates, including degradation, further processing, or serving as functional RNA molecules.

Polyribonucleotide nucleotidyltransferase (PRNT) is not a commonly used medical term, but it is a biological term that refers to an enzyme class with the ability to add nucleotides to the 3'-hydroxyl end of RNA molecules. These enzymes play a crucial role in various cellular processes, including RNA metabolism and repair. They can be found in different organisms, from bacteria to humans.

One well-known example of a PRNT is the RNA polymerase, which synthesizes RNA using DNA as a template during transcription. Another example is the telomere-associated polyribonucleotide nucleotidyltransferase, also known as TERT (telomerase reverse transcriptase), which adds repetitive DNA sequences to the ends of chromosomes (telomeres) to maintain their length and stability.

While PRNTs have significant biological importance, they are not typically referred to in a medical context unless discussing specific diseases or conditions related to their dysfunction.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

Exosomes are small membrane-bound vesicles that are released by many types of cells into the extracellular space. They contain various proteins, lipids, and nucleic acids, including RNA, which can be taken up by other cells and affect their function.

A multienzyme ribonuclease complex is a group of enzymes that work together to degrade RNA.

Therefore, an "Exosome Multienzyme Ribonuclease Complex" refers to the collection of enzymes found within exosomes that are capable of breaking down RNA. These complexes play a role in regulating the levels of RNA both inside and outside of cells, and may also contribute to intercellular communication by transferring functional RNAs between cells.

Ion exchange chromatography is a type of chromatography technique used to separate and analyze charged molecules (ions) based on their ability to exchange bound ions in a solid resin or gel with ions of similar charge in the mobile phase. The stationary phase, often called an ion exchanger, contains fixed ated functional groups that can attract counter-ions of opposite charge from the sample mixture.

In this technique, the sample is loaded onto an ion exchange column containing the charged resin or gel. As the sample moves through the column, ions in the sample compete for binding sites on the stationary phase with ions already present in the column. The ions that bind most strongly to the stationary phase will elute (come off) slower than those that bind more weakly.

Ion exchange chromatography can be performed using either cation exchangers, which exchange positive ions (cations), or anion exchangers, which exchange negative ions (anions). The pH and ionic strength of the mobile phase can be adjusted to control the binding and elution of specific ions.

Ion exchange chromatography is widely used in various applications such as water treatment, protein purification, and chemical analysis.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

Uracil nucleotides are chemical compounds that play a crucial role in the synthesis, repair, and replication of DNA and RNA. Specifically, uracil nucleotides refer to the group of molecules that contain the nitrogenous base uracil, which is linked to a ribose sugar through a beta-glycosidic bond. This forms the nucleoside uridine, which can then be phosphorylated to create the uracil nucleotide.

Uracil nucleotides are important in the formation of RNA, where uracil base pairs with adenine through two hydrogen bonds during transcription. However, uracil is not typically found in DNA, and its presence in DNA can indicate damage or mutation. When uracil is found in DNA, it is usually the result of a process called deamination, where the nitrogenous base cytosine is spontaneously converted to uracil. This can lead to errors during replication, as uracil will pair with adenine instead of guanine, leading to a C-to-T or G-to-A mutation.

To prevent this type of mutation, cells have enzymes called uracil DNA glycosylases that recognize and remove uracil from DNA. This initiates the base excision repair pathway, which removes the damaged nucleotide and replaces it with a correct one. Overall, uracil nucleotides are essential for proper cellular function, but their misincorporation into DNA can have serious consequences for genome stability.

Iodoacetates are salts or esters of iodoacetic acid, an organic compound containing iodine. In medicine, iodoacetates have been used as topical antiseptics and anti-inflammatory agents. However, their use is limited due to potential skin irritation and the availability of safer alternatives.

In a broader context, iodoacetates are also known for their chemical properties. They can act as alkylating agents, which means they can react with proteins and enzymes in living organisms, disrupting their function. This property has been exploited in research to study various cellular processes.

In the context of medicine, "chemistry" often refers to the field of study concerned with the properties, composition, and structure of elements and compounds, as well as their reactions with one another. It is a fundamental science that underlies much of modern medicine, including pharmacology (the study of drugs), toxicology (the study of poisons), and biochemistry (the study of the chemical processes that occur within living organisms).

In addition to its role as a basic science, chemistry is also used in medical testing and diagnosis. For example, clinical chemistry involves the analysis of bodily fluids such as blood and urine to detect and measure various substances, such as glucose, cholesterol, and electrolytes, that can provide important information about a person's health status.

Overall, chemistry plays a critical role in understanding the mechanisms of diseases, developing new treatments, and improving diagnostic tests and techniques.

'Aspergillus oryzae' is a species of filamentous fungi belonging to the family Trichocomaceae. It is commonly known as koji mold and is widely used in the fermentation industry, particularly in Asian countries, for the production of various traditional foods and beverages such as soy sauce, miso, sake, and shochu. The fungus has the ability to produce a variety of enzymes, including amylases, proteases, and lipases, which make it useful in the breakdown and conversion of carbohydrates, proteins, and fats in food substrates.

In addition to its industrial applications, 'Aspergillus oryzae' has also been studied for its potential medicinal properties. Some research suggests that certain compounds produced by the fungus may have antimicrobial, antioxidant, and anti-inflammatory effects. However, more studies are needed to confirm these findings and determine the safety and efficacy of using 'Aspergillus oryzae' for medicinal purposes.

It is worth noting that while 'Aspergillus oryzae' is generally considered safe for food use, it can cause infections in people with weakened immune systems. Therefore, individuals who are at risk of invasive aspergillosis should avoid exposure to this and other species of Aspergillus.

Chemical phenomena refer to the changes and interactions that occur at the molecular or atomic level when chemicals are involved. These phenomena can include chemical reactions, in which one or more substances (reactants) are converted into different substances (products), as well as physical properties that change as a result of chemical interactions, such as color, state of matter, and solubility. Chemical phenomena can be studied through various scientific disciplines, including chemistry, biochemistry, and physics.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Eosinophil granule proteins are a group of biologically active molecules that are stored within the granules of eosinophils, which are types of white blood cells. These proteins include:

1. Eosinophil cationic protein (ECP): A protein with potent ribonuclease activity and the ability to disrupt cell membranes. It is involved in the immune response against parasites and has been implicated in the pathogenesis of several inflammatory diseases, such as asthma and allergies.
2. Eosinophil peroxidase (EPO): An enzyme that generates hypohalous acids, which can cause oxidative damage to cells and tissues. It contributes to the microbicidal activity of eosinophils and has been implicated in the pathogenesis of various inflammatory diseases.
3. Major basic protein (MBP): A highly cationic protein that can disrupt cell membranes, leading to cell lysis. MBP is involved in the immune response against parasites and has been linked to tissue damage in several inflammatory conditions, such as asthma, chronic rhinosinusitis, and eosinophilic esophagitis.
4. Eosinophil-derived neurotoxin (EDN): A protein with ribonuclease activity that can induce histamine release from mast cells and contribute to the inflammatory response. EDN is also involved in the immune response against parasites and has been implicated in the pathogenesis of asthma, allergies, and other inflammatory diseases.

These eosinophil granule proteins are released during eosinophil activation and degranulation, which can occur in response to various stimuli, such as immune complexes, cytokines, and infectious agents. Their release contributes to the inflammatory response and can lead to tissue damage in various diseases.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Cytosine nucleotides are the chemical units or building blocks that make up DNA and RNA, one of the four nitrogenous bases that form the rung of the DNA ladder. A cytosine nucleotide is composed of a cytosine base attached to a sugar molecule (deoxyribose in DNA and ribose in RNA) and at least one phosphate group. The sequence of these nucleotides determines the genetic information stored in an organism's genome. In particular, cytosine nucleotides pair with guanine nucleotides through hydrogen bonding to form base pairs that are held together by weak interactions. This pairing is specific and maintains the structure and integrity of the DNA molecule during replication and transcription.

RNA precursors, also known as primary transcripts or pre-messenger RNAs (pre-mRNAs), refer to the initial RNA molecules that are synthesized during the transcription process in which DNA is copied into RNA. These precursor molecules still contain non-coding sequences and introns, which need to be removed through a process called splicing, before they can become mature and functional RNAs such as messenger RNAs (mRNAs), ribosomal RNAs (rRNAs), or transfer RNAs (tRNAs).

Pre-mRNAs undergo several processing steps, including 5' capping, 3' polyadenylation, and splicing, to generate mature mRNA molecules that can be translated into proteins. The accurate and efficient production of RNA precursors and their subsequent processing are crucial for gene expression and regulation in cells.

Sloths are not a medical term, but rather they refer to slow-moving mammals that live in the trees of Central and South American rainforests. The term "sloth" is used in medicine to describe a state of being, specifically a lack of activity or a delay in making progress or taking action. In this context, it's not related to the animal. If you are looking for information about the sloth animal, I can certainly help with that as well!

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Xenarthra is not a medical term, but a taxonomic category in biology. It refers to the order of mammals that consists of anteaters, sloths, and armadillos. These animals are characterized by their unique skeletal and dental structures, including extra joints between their vertebrae and specialized teeth for grinding or tearing food.

While Xenarthra is not a medical term, it is worth noting that these animals have some unique adaptations that can impact their health and veterinary care. For example, anteaters have an extremely long and sticky tongue to eat ants and termites, which can make dental care challenging. Sloths have a slow metabolism and spend most of their time hanging upside down in trees, which can affect their digestion and musculoskeletal health. Armadillos are known to be carriers of leprosy, which can impact human health in certain areas where they are common.

Magnesium is an essential mineral that plays a crucial role in various biological processes in the human body. It is the fourth most abundant cation in the body and is involved in over 300 enzymatic reactions, including protein synthesis, muscle and nerve function, blood glucose control, and blood pressure regulation. Magnesium also contributes to the structural development of bones and teeth.

In medical terms, magnesium deficiency can lead to several health issues, such as muscle cramps, weakness, heart arrhythmias, and seizures. On the other hand, excessive magnesium levels can cause symptoms like diarrhea, nausea, and muscle weakness. Magnesium supplements or magnesium-rich foods are often recommended to maintain optimal magnesium levels in the body.

Some common dietary sources of magnesium include leafy green vegetables, nuts, seeds, legumes, whole grains, and dairy products. Magnesium is also available in various forms as a dietary supplement, including magnesium oxide, magnesium citrate, magnesium chloride, and magnesium glycinate.

Oligonucleotides are short sequences of nucleotides, the building blocks of DNA and RNA. They typically contain fewer than 100 nucleotides, and can be synthesized chemically to have specific sequences. Oligonucleotides are used in a variety of applications in molecular biology, including as probes for detecting specific DNA or RNA sequences, as inhibitors of gene expression, and as components of diagnostic tests and therapies. They can also be used in the study of protein-nucleic acid interactions and in the development of new drugs.

Ribosomes are complex macromolecular structures composed of ribonucleic acid (RNA) and proteins that play a crucial role in protein synthesis within cells. They serve as the site for translation, where messenger RNA (mRNA) is translated into a specific sequence of amino acids to create a polypeptide chain, which eventually folds into a functional protein.

Ribosomes consist of two subunits: a smaller subunit and a larger subunit. These subunits are composed of ribosomal RNA (rRNA) molecules and proteins. In eukaryotic cells, the smaller subunit is denoted as the 40S subunit, while the larger subunit is referred to as the 60S subunit. In prokaryotic cells, these subunits are named the 30S and 50S subunits, respectively. The ribosome's overall structure resembles a "doughnut" or a "cotton reel," with grooves and binding sites for various factors involved in protein synthesis.

Ribosomes can be found floating freely within the cytoplasm of cells or attached to the endoplasmic reticulum (ER) membrane, forming part of the rough ER. Membrane-bound ribosomes are responsible for synthesizing proteins that will be transported across the ER and ultimately secreted from the cell or inserted into the membrane. In contrast, cytoplasmic ribosomes synthesize proteins destined for use within the cytoplasm or organelles.

In summary, ribosomes are essential components of cells that facilitate protein synthesis by translating mRNA into functional polypeptide chains. They can be found in various cellular locations and exist as either free-floating entities or membrane-bound structures.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

I'm sorry for any confusion, but "thermodynamics" is not a term that has a specific medical definition. It is a branch of physics that deals with the relationships between heat and other forms of energy. However, the principles of thermodynamics can be applied to biological systems, including those in the human body, such as in the study of metabolism or muscle function. But in a medical context, "thermodynamics" would not be a term used independently as a diagnosis, treatment, or any medical condition.

'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.

E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.

Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.

Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

Uridine is a nucleoside that consists of a pyrimidine base (uracil) linked to a pentose sugar (ribose). It is a component of RNA, where it pairs with adenine. Uridine can also be found in various foods such as beer, broccoli, yeast, and meat. In the body, uridine can be synthesized from orotate or from the breakdown of RNA. It has several functions, including acting as a building block for RNA, contributing to energy metabolism, and regulating cell growth and differentiation. Uridine is also available as a dietary supplement and has been studied for its potential benefits in various health conditions.

Post-transcriptional RNA processing refers to the modifications and regulations that occur on RNA molecules after the transcription of DNA into RNA. This process includes several steps:

1. 5' capping: The addition of a cap structure, usually a methylated guanosine triphosphate (GTP), to the 5' end of the RNA molecule. This helps protect the RNA from degradation and plays a role in its transport, stability, and translation.
2. 3' polyadenylation: The addition of a string of adenosine residues (poly(A) tail) to the 3' end of the RNA molecule. This process is important for mRNA stability, export from the nucleus, and translation initiation.
3. Intron removal and exon ligation: Eukaryotic pre-messenger RNAs (pre-mRNAs) contain intronic sequences that do not code for proteins. These introns are removed by a process called splicing, where the flanking exons are joined together to form a continuous mRNA sequence. Alternative splicing can lead to different mature mRNAs from a single pre-mRNA, increasing transcriptomic and proteomic diversity.
4. RNA editing: Specific nucleotide changes in RNA molecules that alter the coding potential or regulatory functions of RNA. This process is catalyzed by enzymes like ADAR (Adenosine Deaminases Acting on RNA) and APOBEC (Apolipoprotein B mRNA Editing Catalytic Polypeptide-like).
5. Chemical modifications: Various chemical modifications can occur on RNA nucleotides, such as methylation, pseudouridination, and isomerization. These modifications can influence RNA stability, localization, and interaction with proteins or other RNAs.
6. Transport and localization: Mature mRNAs are transported from the nucleus to the cytoplasm for translation. In some cases, specific mRNAs are localized to particular cellular compartments to ensure local protein synthesis.
7. Degradation: RNA molecules have finite lifetimes and undergo degradation by various ribonucleases (RNases). The rate of degradation can be influenced by factors such as RNA structure, modifications, or interactions with proteins.

In a medical context, "hot temperature" is not a standard medical term with a specific definition. However, it is often used in relation to fever, which is a common symptom of illness. A fever is typically defined as a body temperature that is higher than normal, usually above 38°C (100.4°F) for adults and above 37.5-38°C (99.5-101.3°F) for children, depending on the source.

Therefore, when a medical professional talks about "hot temperature," they may be referring to a body temperature that is higher than normal due to fever or other causes. It's important to note that a high environmental temperature can also contribute to an elevated body temperature, so it's essential to consider both the body temperature and the environmental temperature when assessing a patient's condition.

Divalent cations are ions that carry a positive charge of +2. They are called divalent because they have two positive charges. Common examples of divalent cations include calcium (Ca²+), magnesium (Mg²+), and iron (Fe²+). These ions play important roles in various biological processes, such as muscle contraction, nerve impulse transmission, and bone metabolism. They can also interact with certain drugs and affect their absorption, distribution, and elimination in the body.

Dinucleoside phosphates are the chemical compounds that result from the linkage of two nucleosides through a phosphate group. Nucleosides themselves consist of a sugar molecule (ribose or deoxyribose) and a nitrogenous base (adenine, guanine, cytosine, thymine, or uracil). When two nucleosides are joined together by an ester bond between the phosphate group and the 5'-hydroxyl group of the sugar moiety, they form a dinucleoside phosphate.

These compounds play crucial roles in various biological processes, particularly in the context of DNA and RNA synthesis and repair. For instance, dinucleoside phosphates serve as building blocks for the formation of longer nucleic acid chains during replication and transcription. They are also involved in signaling pathways and energy transfer within cells.

It is worth noting that the term "dinucleotides" is sometimes used interchangeably with dinucleoside phosphates, although technically, dinucleotides refer to compounds formed by joining two nucleotides (nucleosides plus one or more phosphate groups) rather than just two nucleosides.

Thermolysin is not a medical term per se, but it is a bacterial enzyme that is often used in biochemistry and molecular biology research. Here's the scientific or biochemical definition:

Thermolysin is a zinc metalloprotease enzyme produced by the bacteria Geobacillus stearothermophilus. It has an optimum temperature for activity at around 65°C, and it can remain active in high temperatures, which makes it useful in various industrial applications. Thermolysin is known for its ability to cleave peptide bonds, particularly those involving hydrophobic residues, making it a valuable tool in protein research and engineering.

Eosinophil Cationic Protein (ECP) is a protein found in the granules of eosinophils, which are a type of white blood cell that plays a role in the immune response, particularly against parasitic infections and allergens. ECP is released from eosinophils during degranulation, a process that occurs when these cells are activated and release their granules' contents.

Elevated levels of ECP in body fluids, such as blood or sputum, can indicate eosinophil activation and may be associated with various inflammatory conditions, including asthma, allergies, and some parasitic infections. Measuring ECP levels can help monitor disease activity and assess the effectiveness of treatment in these conditions.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Nucleic acid denaturation is the process of separating the two strands of a double-stranded DNA molecule, or unwinding the helical structure of an RNA molecule, by disrupting the hydrogen bonds that hold the strands together. This process is typically caused by exposure to high temperatures, changes in pH, or the presence of chemicals called denaturants.

Denaturation can also cause changes in the shape and function of nucleic acids. For example, it can disrupt the secondary and tertiary structures of RNA molecules, which can affect their ability to bind to other molecules and carry out their functions within the cell.

In molecular biology, nucleic acid denaturation is often used as a tool for studying the structure and function of nucleic acids. For example, it can be used to separate the two strands of a DNA molecule for sequencing or amplification, or to study the interactions between nucleic acids and other molecules.

It's important to note that denaturation is a reversible process, and under the right conditions, the double-stranded structure of DNA can be restored through a process called renaturation or annealing.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

RNA-directed DNA polymerase is a type of enzyme that can synthesize DNA using an RNA molecule as a template. This process is called reverse transcription, and it is the mechanism by which retroviruses, such as HIV, replicate their genetic material. The enzyme responsible for this reaction in retroviruses is called reverse transcriptase.

Reverse transcriptase is an important target for antiretroviral therapy used to treat HIV infection and AIDS. In addition to its role in viral replication, RNA-directed DNA polymerase also has applications in molecular biology research, such as in the production of complementary DNA (cDNA) copies of RNA molecules for use in downstream applications like cloning and sequencing.

I'm happy to help! However, it seems there might be a slight misunderstanding in your question. RNA, or ribonucleic acid, is typically single-stranded. Unlike DNA, which is double-stranded and forms a double helix, RNA usually exists as a single strand of nucleotides.

There are exceptions to this rule, such as certain types of RNA molecules that can form double-stranded structures in specific contexts. For example:

1. Double-Stranded RNA (dsRNA) viruses: These viruses have genomes made entirely of RNA, which is double-stranded throughout or partially double-stranded. The dsRNA viruses include important pathogens such as rotaviruses and reoviruses.
2. Hairpin loops in RNA structures: Some single-stranded RNA molecules can fold back on themselves to form short double-stranded regions, called hairpin loops, within their overall structure. These are often found in ribosomal RNA (rRNA), transfer RNA (tRNA), and messenger RNA (mRNA) molecules.

So, while 'double-stranded RNA' is not a standard medical definition for RNA itself, there are specific instances where RNA can form double-stranded structures as described above.

I'm sorry for any confusion, but "Poly U" is not a recognized medical term or abbreviation in the English language. It could potentially refer to Polytechnic University or Hong Kong Polytechnic University, but it does not have a specific medical connotation. If you have more context or information, I'd be happy to help further!

"Streptomyces aureofaciens" is a species of aerobic, gram-positive bacteria belonging to the family Streptomycetaceae. These bacteria are known for their ability to produce a variety of bioactive secondary metabolites, including antibiotics and enzymes. "Streptomyces aureofaciens" is particularly known for producing the antibiotic undecylenic acid, which has antifungal properties. The bacteria are commonly found in soil and aquatic environments.

It's important to note that while I strive to provide accurate and up-to-date information, this definition may not be fully comprehensive or suitable for all purposes. For a more detailed and professional understanding, it is recommended to consult authoritative medical and scientific resources or speak with a healthcare provider or scientist in the field.

RNA stability refers to the duration that a ribonucleic acid (RNA) molecule remains intact and functional within a cell before it is degraded or broken down into its component nucleotides. Various factors can influence RNA stability, including:

1. Primary sequence: Certain sequences in the RNA molecule may be more susceptible to degradation by ribonucleases (RNases), enzymes that break down RNA.
2. Secondary structure: The formation of stable secondary structures, such as hairpins or stem-loop structures, can protect RNA from degradation.
3. Presence of RNA-binding proteins: Proteins that bind to RNA can either stabilize or destabilize the RNA molecule, depending on the type and location of the protein-RNA interaction.
4. Chemical modifications: Modifications to the RNA nucleotides, such as methylation, can increase RNA stability by preventing degradation.
5. Subcellular localization: The subcellular location of an RNA molecule can affect its stability, with some locations providing more protection from ribonucleases than others.
6. Cellular conditions: Changes in cellular conditions, such as pH or temperature, can also impact RNA stability.

Understanding RNA stability is important for understanding gene regulation and the function of non-coding RNAs, as well as for developing RNA-based therapeutic strategies.

Hydrogen bonding is not a medical term per se, but it is a fundamental concept in chemistry and biology that is relevant to the field of medicine. Here's a general definition:

Hydrogen bonding is a type of attractive force between molecules or within a molecule, which occurs when a hydrogen atom is bonded to a highly electronegative atom (like nitrogen, oxygen, or fluorine) and is then attracted to another electronegative atom. This attraction results in the formation of a partially covalent bond known as a "hydrogen bond."

In biological systems, hydrogen bonding plays a crucial role in the structure and function of many biomolecules, such as DNA, proteins, and carbohydrates. For example, the double helix structure of DNA is stabilized by hydrogen bonds between complementary base pairs (adenine-thymine and guanine-cytosine). Similarly, the three-dimensional structure of proteins is maintained by a network of hydrogen bonds that help to determine their function.

In medical contexts, hydrogen bonding can be relevant in understanding drug-receptor interactions, where hydrogen bonds between a drug molecule and its target protein can enhance the binding affinity and specificity of the interaction, leading to more effective therapeutic outcomes.

Ribonucleoproteins (RNPs) are complexes composed of ribonucleic acid (RNA) and proteins. They play crucial roles in various cellular processes, including gene expression, RNA processing, transport, stability, and degradation. Different types of RNPs exist, such as ribosomes, spliceosomes, and signal recognition particles, each having specific functions in the cell.

Ribosomes are large RNP complexes responsible for protein synthesis, where messenger RNA (mRNA) is translated into proteins. They consist of two subunits: a smaller subunit containing ribosomal RNA (rRNA) and proteins that recognize the start codon on mRNA, and a larger subunit with rRNA and proteins that facilitate peptide bond formation during translation.

Spliceosomes are dynamic RNP complexes involved in pre-messenger RNA (pre-mRNA) splicing, where introns (non-coding sequences) are removed, and exons (coding sequences) are joined together to form mature mRNA. Spliceosomes consist of five small nuclear ribonucleoproteins (snRNPs), each containing a specific small nuclear RNA (snRNA) and several proteins, as well as numerous additional proteins.

Other RNP complexes include signal recognition particles (SRPs), which are responsible for targeting secretory and membrane proteins to the endoplasmic reticulum during translation, and telomerase, an enzyme that maintains the length of telomeres (the protective ends of chromosomes) by adding repetitive DNA sequences using its built-in RNA component.

In summary, ribonucleoproteins are essential complexes in the cell that participate in various aspects of RNA metabolism and protein synthesis.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Trypsin is a proteolytic enzyme, specifically a serine protease, that is secreted by the pancreas as an inactive precursor, trypsinogen. Trypsinogen is converted into its active form, trypsin, in the small intestine by enterokinase, which is produced by the intestinal mucosa.

Trypsin plays a crucial role in digestion by cleaving proteins into smaller peptides at specific arginine and lysine residues. This enzyme helps to break down dietary proteins into amino acids, allowing for their absorption and utilization by the body. Additionally, trypsin can activate other zymogenic pancreatic enzymes, such as chymotrypsinogen and procarboxypeptidases, thereby contributing to overall protein digestion.

Guanidine is not typically defined in the context of medical terminology, but rather, it is a chemical compound with the formula NH2(C=NH)NH2. However, guanidine and its derivatives do have medical relevance:

1. Guanidine is used as a medication in some neurological disorders, such as stiff-person syndrome, to reduce muscle spasms and rigidity. It acts on the central nervous system to decrease abnormal nerve impulses that cause muscle spasticity.

2. Guanidine derivatives are found in various medications used for treating diabetes, like metformin. These compounds help lower glucose production in the liver and improve insulin sensitivity in muscle cells.

3. In some cases, guanidine is used as a skin penetration enhancer in transdermal drug delivery systems to increase the absorption of certain medications through the skin.

It is essential to note that guanidine itself has limited medical use due to its potential toxicity and narrow therapeutic window. Its derivatives, like metformin, are more commonly used in medical practice.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Muramidase, also known as lysozyme, is an enzyme that hydrolyzes the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, a polymer found in bacterial cell walls. This enzymatic activity plays a crucial role in the innate immune system by contributing to the destruction of invading bacteria. Muramidase is widely distributed in various tissues and bodily fluids, such as tears, saliva, and milk, and is also found in several types of white blood cells, including neutrophils and monocytes.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

A viral RNA (ribonucleic acid) is the genetic material found in certain types of viruses, as opposed to viruses that contain DNA (deoxyribonucleic acid). These viruses are known as RNA viruses. The RNA can be single-stranded or double-stranded and can exist as several different forms, such as positive-sense, negative-sense, or ambisense RNA. Upon infecting a host cell, the viral RNA uses the host's cellular machinery to translate the genetic information into proteins, leading to the production of new virus particles and the continuation of the viral life cycle. Examples of human diseases caused by RNA viruses include influenza, COVID-19 (SARS-CoV-2), hepatitis C, and polio.

Rhizopus is a genus of saprophytic fungi that belong to the family Mucoraceae. These fungi are commonly found in soil, decaying vegetation, and fruits. They are characterized by the presence of rhizoids, which are multicellular filaments that anchor the fungus to its substrate.

Rhizopus species are known to produce spores in large numbers, which can be dispersed through the air and cause infections in humans, particularly in individuals with weakened immune systems. One of the most common diseases caused by Rhizopus is mucormycosis, a serious and often life-threatening fungal infection that can affect various organs, including the sinuses, lungs, brain, and skin.

It's worth noting that while Rhizopus species are important pathogens in certain populations, they also have beneficial uses. For example, some species of Rhizopus are used in the production of tempeh, a traditional Indonesian food made from fermented soybeans.

Transfer RNA (tRNA) that specifically carries the amino acid tyrosine (Tyr) during protein synthesis. In genetic code, Tyr is coded by the codons UAC and UAU. The corresponding anticodon on the tRNA molecule is AUA, which pairs with the mRNA codons to bring tyrosine to the ribosome for incorporation into the growing polypeptide chain.

Urea is not a medical condition but it is a medically relevant substance. Here's the definition:

Urea is a colorless, odorless solid that is the primary nitrogen-containing compound in the urine of mammals. It is a normal metabolic end product that is excreted by the kidneys and is also used as a fertilizer and in various industrial applications. Chemically, urea is a carbamide, consisting of two amino groups (NH2) joined by a carbon atom and having a hydrogen atom and a hydroxyl group (OH) attached to the carbon atom. Urea is produced in the liver as an end product of protein metabolism and is then eliminated from the body by the kidneys through urination. Abnormal levels of urea in the blood, known as uremia, can indicate impaired kidney function or other medical conditions.

"Aspergillus" is a genus of filamentous fungi (molds) that are widely distributed in the environment. These molds are commonly found in decaying organic matter such as leaf litter, compost piles, and rotting vegetation. They can also be found in indoor environments like air conditioning systems, dust, and building materials.

The medical relevance of Aspergillus comes from the fact that some species can cause a range of diseases in humans, particularly in individuals with weakened immune systems or underlying lung conditions. The most common disease caused by Aspergillus is called aspergillosis, which can manifest as allergic reactions, lung infections (like pneumonia), and invasive infections that can spread to other parts of the body.

Aspergillus species produce small, airborne spores called conidia, which can be inhaled into the lungs and cause infection. The severity of aspergillosis depends on various factors, including the individual's immune status, the specific Aspergillus species involved, and the extent of fungal invasion in the body.

Common Aspergillus species that can cause human disease include A. fumigatus, A. flavus, A. niger, and A. terreus. Preventing exposure to Aspergillus spores and maintaining a healthy immune system are crucial steps in minimizing the risk of aspergillosis.

Chromatography is a technique used in analytical chemistry for the separation, identification, and quantification of the components of a mixture. It is based on the differential distribution of the components of a mixture between a stationary phase and a mobile phase. The stationary phase can be a solid or liquid, while the mobile phase is a gas, liquid, or supercritical fluid that moves through the stationary phase carrying the sample components.

The interaction between the sample components and the stationary and mobile phases determines how quickly each component will move through the system. Components that interact more strongly with the stationary phase will move more slowly than those that interact more strongly with the mobile phase. This difference in migration rates allows for the separation of the components, which can then be detected and quantified.

There are many different types of chromatography, including paper chromatography, thin-layer chromatography (TLC), gas chromatography (GC), liquid chromatography (LC), and high-performance liquid chromatography (HPLC). Each type has its own strengths and weaknesses, and is best suited for specific applications.

In summary, chromatography is a powerful analytical technique used to separate, identify, and quantify the components of a mixture based on their differential distribution between a stationary phase and a mobile phase.

Tritium is not a medical term, but it is a term used in the field of nuclear physics and chemistry. Tritium (symbol: T or 3H) is a radioactive isotope of hydrogen with two neutrons and one proton in its nucleus. It is also known as heavy hydrogen or superheavy hydrogen.

Tritium has a half-life of about 12.3 years, which means that it decays by emitting a low-energy beta particle (an electron) to become helium-3. Due to its radioactive nature and relatively short half-life, tritium is used in various applications, including nuclear weapons, fusion reactors, luminous paints, and medical research.

In the context of medicine, tritium may be used as a radioactive tracer in some scientific studies or medical research, but it is not a term commonly used to describe a medical condition or treatment.

I'm sorry for any confusion, but "Poly I" is not a recognized medical term or abbreviation in the context of human diseases or conditions. It's possible that there might be a typo or misunderstanding in your query. If you intended to ask about a specific medical condition, medication, or concept, please provide the full and correct term so I can give you an accurate and helpful response.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

Uridine Monophosphate (UMP) is a nucleotide that is a constituent of RNA (Ribonucleic Acid). It consists of a nitrogenous base called Uridine, linked to a sugar molecule (ribose) and a phosphate group. UMP plays a crucial role in various biochemical reactions within the body, including energy transfer and cellular metabolism. It is also involved in the synthesis of other nucleotides and serves as an important precursor in the production of genetic material during cell division.

Guanidines are organic compounds that contain a guanidino group, which is a functional group with the formula -NH-C(=NH)-NH2. Guanidines can be found in various natural sources, including some animals, plants, and microorganisms. They also occur as byproducts of certain metabolic processes in the body.

In a medical context, guanidines are most commonly associated with the treatment of muscle weakness and neuromuscular disorders. The most well-known guanidine compound is probably guanidine hydrochloride, which has been used as a medication to treat conditions such as myasthenia gravis and Eaton-Lambert syndrome.

However, the use of guanidines as medications has declined in recent years due to their potential for toxicity and the development of safer and more effective treatments. Today, guanidines are mainly used in research settings to study various biological processes, including protein folding and aggregation, enzyme inhibition, and cell signaling.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Disulfides are a type of organic compound that contains a sulfur-sulfur bond. In the context of biochemistry and medicine, disulfide bonds are often found in proteins, where they play a crucial role in maintaining their three-dimensional structure and function. These bonds form when two sulfhydryl groups (-SH) on cysteine residues within a protein molecule react with each other, releasing a molecule of water and creating a disulfide bond (-S-S-) between the two cysteines. Disulfide bonds can be reduced back to sulfhydryl groups by various reducing agents, which is an important process in many biological reactions. The formation and reduction of disulfide bonds are critical for the proper folding, stability, and activity of many proteins, including those involved in various physiological processes and diseases.

Nuclease protection assays are a type of molecular biology technique used to identify and quantify specific nucleic acid sequences, such as DNA or RNA. This assay involves the use of nuclease enzymes that can cut or degrade single-stranded nucleic acids, but not double-stranded ones.

In a typical nuclease protection assay, a labeled probe complementary to the target nucleic acid sequence is hybridized to the sample RNA or DNA. The sample is then treated with single-strand specific nucleases, which digest any unhybridized single-stranded nucleic acids. The double-stranded regions protected by the hybridization of the labeled probe are then isolated and analyzed, often using gel electrophoresis or other detection methods.

The length and intensity of the resulting protected fragments can provide information about the size, location, and abundance of the target nucleic acid sequence in the sample. Nuclease protection assays are commonly used to study gene expression, RNA processing, and other aspects of molecular biology.

DEAE-cellulose chromatography is a method of purification and separation of biological molecules such as proteins, nucleic acids, and enzymes. DEAE stands for diethylaminoethyl, which is a type of charged functional group that is covalently bound to cellulose, creating a matrix with positive charges.

In this method, the mixture of biological molecules is applied to a column packed with DEAE-cellulose. The positively charged DEAE groups attract and bind negatively charged molecules in the mixture, such as nucleic acids and proteins, while allowing uncharged or neutrally charged molecules to pass through.

By adjusting the pH, ionic strength, or concentration of salt in the buffer solution used to elute the bound molecules from the column, it is possible to selectively elute specific molecules based on their charge and binding affinity to the DEAE-cellulose matrix. This makes DEAE-cellulose chromatography a powerful tool for purifying and separating biological molecules with high resolution and efficiency.

Phosphorus isotopes are different forms of the element phosphorus that have different numbers of neutrons in their atomic nuclei, while the number of protons remains the same. The most common and stable isotope of phosphorus is 31P, which contains 15 protons and 16 neutrons. However, there are also several other isotopes of phosphorus that exist, including 32P and 33P, which are radioactive and have 15 protons and 17 or 18 neutrons, respectively. These radioactive isotopes are often used in medical research and treatment, such as in the form of radiopharmaceuticals to diagnose and treat various diseases.

"Poly A" is an abbreviation for "poly(A) tail" or "polyadenylation." It refers to the addition of multiple adenine (A) nucleotides to the 3' end of eukaryotic mRNA molecules during the process of transcription. This poly(A) tail plays a crucial role in various aspects of mRNA metabolism, including stability, transport, and translation. The length of the poly(A) tail can vary from around 50 to 250 nucleotides depending on the cell type and developmental stage.

X-ray diffraction (XRD) is not strictly a medical definition, but it is a technique commonly used in the field of medical research and diagnostics. XRD is a form of analytical spectroscopy that uses the phenomenon of X-ray diffraction to investigate the crystallographic structure of materials. When a beam of X-rays strikes a crystal, it is scattered in specific directions and with specific intensities that are determined by the arrangement of atoms within the crystal. By measuring these diffraction patterns, researchers can determine the crystal structures of various materials, including biological macromolecules such as proteins and viruses.

In the medical field, XRD is often used to study the structure of drugs and drug candidates, as well as to analyze the composition and structure of tissues and other biological samples. For example, XRD can be used to investigate the crystal structures of calcium phosphate minerals in bone tissue, which can provide insights into the mechanisms of bone formation and disease. Additionally, XRD is sometimes used in the development of new medical imaging techniques, such as phase-contrast X-ray imaging, which has the potential to improve the resolution and contrast of traditional X-ray images.

Paper chromatography is a type of chromatography technique that involves the separation and analysis of mixtures based on their components' ability to migrate differently upon capillary action on a paper medium. This simple and cost-effective method utilizes a paper, typically made of cellulose, as the stationary phase. The sample mixture is applied as a small spot near one end of the paper, and then the other end is dipped into a developing solvent or a mixture of solvents (mobile phase) in a shallow container.

As the mobile phase moves up the paper by capillary action, components within the sample mixture separate based on their partition coefficients between the stationary and mobile phases. The partition coefficient describes how much a component prefers to be in either the stationary or mobile phase. Components with higher partition coefficients in the mobile phase will move faster and further than those with lower partition coefficients.

Once separation is complete, the paper is dried and can be visualized under ultraviolet light or by using chemical reagents specific for the components of interest. The distance each component travels from the origin (point of application) and its corresponding solvent front position are measured, allowing for the calculation of Rf values (retardation factors). Rf is a dimensionless quantity calculated as the ratio of the distance traveled by the component to the distance traveled by the solvent front.

Rf = (distance traveled by component) / (distance traveled by solvent front)

Paper chromatography has been widely used in various applications, such as:

1. Identification and purity analysis of chemical compounds in pharmaceuticals, forensics, and research laboratories.
2. Separation and detection of amino acids, sugars, and other biomolecules in biological samples.
3. Educational purposes to demonstrate the principles of chromatography and separation techniques.

Despite its limitations, such as lower resolution compared to high-performance liquid chromatography (HPLC) and less compatibility with volatile or nonpolar compounds, paper chromatography remains a valuable tool for quick, qualitative analysis in various fields.

Semen is a complex, whitish fluid that is released from the male reproductive system during ejaculation. It is produced by several glands, including the seminal vesicles, prostate gland, and bulbourethral glands. Semen contains several components, including sperm (the male reproductive cells), as well as various proteins, enzymes, vitamins, and minerals. Its primary function is to transport sperm through the female reproductive tract during sexual intercourse, providing nutrients and aiding in the protection of the sperm as they travel toward the egg for fertilization.

RNA probes are specialized biomolecules used in molecular biology to detect and localize specific RNA sequences within cells or tissues. They are typically single-stranded RNA molecules that have been synthesized with a modified nucleotide, such as digoxigenin or biotin, which can be detected using antibodies or streptavidin conjugates.

RNA probes are used in techniques such as in situ hybridization (ISH) and Northern blotting to identify the spatial distribution of RNA transcripts within cells or tissues, or to quantify the amount of specific RNA present in a sample. The probe is designed to be complementary to the target RNA sequence, allowing it to bind specifically to its target through base-pairing interactions.

RNA probes can be labeled with various reporter molecules, such as radioactive isotopes or fluorescent dyes, which enable their detection and visualization using techniques such as autoradiography or microscopy. The use of RNA probes has proven to be a valuable tool in the study of gene expression, regulation, and localization in various biological systems.

Guanine nucleotides are molecules that play a crucial role in intracellular signaling, cellular regulation, and various biological processes within cells. They consist of a guanine base, a sugar (ribose or deoxyribose), and one or more phosphate groups. The most common guanine nucleotides are GDP (guanosine diphosphate) and GTP (guanosine triphosphate).

GTP is hydrolyzed to GDP and inorganic phosphate by certain enzymes called GTPases, releasing energy that drives various cellular functions such as protein synthesis, signal transduction, vesicle transport, and cell division. On the other hand, GDP can be rephosphorylated back to GTP by nucleotide diphosphate kinases, allowing for the recycling of these molecules within the cell.

In addition to their role in signaling and regulation, guanine nucleotides also serve as building blocks for RNA (ribonucleic acid) synthesis during transcription, where they pair with cytosine nucleotides via hydrogen bonds to form base pairs in the resulting RNA molecule.

Ribonucleotides are organic compounds that consist of a ribose sugar, a phosphate group, and a nitrogenous base. They are the building blocks of RNA (ribonucleic acid), one of the essential molecules in all living organisms. The nitrogenous bases found in ribonucleotides include adenine, uracil, guanine, and cytosine. These molecules play crucial roles in various biological processes, such as protein synthesis, gene expression, and cellular energy production. Ribonucleotides can also be involved in cell signaling pathways and serve as important cofactors for enzymatic reactions.

Basidiomycota is a phylum in the kingdom Fungi that consists of organisms commonly known as club fungi or club mushrooms. The name Basidiomycota is derived from the presence of a characteristic reproductive structure called a basidium, which is where spores are produced.

The basidiomycetes include many familiar forms such as mushrooms, toadstools, bracket fungi, and other types of polypores. They have a complex life cycle that involves both sexual and asexual reproduction. The sexual reproductive stage produces a characteristic fruiting body, which may be microscopic or highly visible, depending on the species.

Basidiomycota fungi play important ecological roles in decomposing organic matter, forming mutualistic relationships with plants, and acting as parasites on other organisms. Some species are economically important, such as edible mushrooms, while others can be harmful or even deadly to humans and animals.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

Proflavine is an antimicrobial agent, specifically a type of dye known as an acridine dye. It is used primarily as a topical antiseptic and disinfectant. Proflavine works by intercalating into DNA, which disrupts the structure of the DNA molecule and prevents bacterial replication.

It's important to note that proflavine has been largely replaced by other more effective and safer antimicrobial agents in clinical practice. It is still used in some research settings and for certain specific applications, such as staining tissues for microscopic examination.

Proflavine should be used with caution, as it can cause skin irritation and may have harmful effects if ingested or absorbed through the skin. As with any medication, it should only be used under the guidance of a healthcare professional.

Electrophoresis is a laboratory technique used in the field of molecular biology and chemistry to separate charged particles, such as DNA, RNA, or proteins, based on their size and charge. This technique uses an electric field to drive the movement of these charged particles through a medium, such as gel or liquid.

In electrophoresis, the sample containing the particles to be separated is placed in a matrix, such as a gel or a capillary tube, and an electric current is applied. The particles in the sample have a net charge, either positive or negative, which causes them to move through the matrix towards the oppositely charged electrode.

The rate at which the particles move through the matrix depends on their size and charge. Larger particles move more slowly than smaller ones, and particles with a higher charge-to-mass ratio move faster than those with a lower charge-to-mass ratio. By comparing the distance that each particle travels in the matrix, researchers can identify and quantify the different components of a mixture.

Electrophoresis has many applications in molecular biology and medicine, including DNA sequencing, genetic fingerprinting, protein analysis, and diagnosis of genetic disorders.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Nucleic acid hybridization is a process in molecular biology where two single-stranded nucleic acids (DNA, RNA) with complementary sequences pair together to form a double-stranded molecule through hydrogen bonding. The strands can be from the same type of nucleic acid or different types (i.e., DNA-RNA or DNA-cDNA). This process is commonly used in various laboratory techniques, such as Southern blotting, Northern blotting, polymerase chain reaction (PCR), and microarray analysis, to detect, isolate, and analyze specific nucleic acid sequences. The hybridization temperature and conditions are critical to ensure the specificity of the interaction between the two strands.

Chymotrypsin is a proteolytic enzyme, specifically a serine protease, that is produced in the pancreas and secreted into the small intestine as an inactive precursor called chymotrypsinogen. Once activated, chymotrypsin helps to digest proteins in food by breaking down specific peptide bonds in protein molecules. Its activity is based on the recognition of large hydrophobic side chains in amino acids like phenylalanine, tryptophan, and tyrosine. Chymotrypsin plays a crucial role in maintaining normal digestion and absorption processes in the human body.

Nucleotides are the basic structural units of nucleic acids, such as DNA and RNA. They consist of a nitrogenous base (adenine, guanine, cytosine, thymine or uracil), a pentose sugar (ribose in RNA and deoxyribose in DNA) and one to three phosphate groups. Nucleotides are linked together by phosphodiester bonds between the sugar of one nucleotide and the phosphate group of another, forming long chains known as polynucleotides. The sequence of these nucleotides determines the genetic information carried in DNA and RNA, which is essential for the functioning, reproduction and survival of all living organisms.

A chemical model is a simplified representation or description of a chemical system, based on the laws of chemistry and physics. It is used to explain and predict the behavior of chemicals and chemical reactions. Chemical models can take many forms, including mathematical equations, diagrams, and computer simulations. They are often used in research, education, and industry to understand complex chemical processes and develop new products and technologies.

For example, a chemical model might be used to describe the way that atoms and molecules interact in a particular reaction, or to predict the properties of a new material. Chemical models can also be used to study the behavior of chemicals at the molecular level, such as how they bind to each other or how they are affected by changes in temperature or pressure.

It is important to note that chemical models are simplifications of reality and may not always accurately represent every aspect of a chemical system. They should be used with caution and validated against experimental data whenever possible.

Protein Disulfide-Isomerases (PDIs) are a family of enzymes found in the endoplasmic reticulum (ER) of eukaryotic cells. They play a crucial role in the folding and maturation of proteins by catalyzing the formation, breakage, and rearrangement of disulfide bonds between cysteine residues in proteins. This process helps to stabilize the three-dimensional structure of proteins and is essential for their proper function. PDIs also have chaperone activity, helping to prevent protein aggregation and assisting in the correct folding of nascent polypeptides. Dysregulation of PDI function has been implicated in various diseases, including cancer, neurodegenerative disorders, and diabetes.

I believe there may be a slight error in the term you're asking about. "Asp" doesn't specifically relate to RNA (Ribonucleic Acid) or its types. However, I can provide a definition for "Transfer RNA" (tRNA).

Transfer RNA (tRNA) is a type of RNA that plays a crucial role in protein synthesis. It carries and transfers specific amino acids to the growing polypeptide chain during translation, according to the genetic code provided by messenger RNA (mRNA). Each tRNA molecule has an anticodon region which can base-pair with a complementary codon in the mRNA, and a corresponding amino acid attached to its other end. This enables the correct matching of amino acids to form proteins according to the genetic information encoded in mRNA.

HIV Reverse Transcriptase is an enzyme that is encoded by the HIV-1 and HIV-2 viruses. It plays a crucial role in the replication cycle of the human immunodeficiency virus (HIV), which causes AIDS.

Reverse transcriptase is responsible for transcribing the viral RNA genome into DNA, a process known as reverse transcription. This allows the viral genetic material to integrate into the host cell's DNA and replicate along with it, leading to the production of new virus particles.

The enzyme has three distinct activities: a polymerase activity that synthesizes DNA using RNA as a template, an RNase H activity that degrades the RNA template during reverse transcription, and a DNA-dependent DNA polymerase activity that synthesizes DNA using a DNA template.

Reverse transcriptase inhibitors are a class of antiretroviral drugs used to treat HIV infection. They work by binding to and inhibiting the activity of the reverse transcriptase enzyme, thereby preventing the virus from replicating.

"Poly A-U" is not a standard medical term. However, in biochemistry and genetics, "poly A" and "poly U" refer to repeating sequences of adenine (A) or uracil (U) nucleotides in DNA or RNA molecules, respectively.

"Poly A" is a post-transcriptional modification that occurs in mRNA, where multiple adenine nucleotides are added to the 3' end of the transcript. This process is important for the stability and translation of mRNA in eukaryotic cells.

"Poly U," on the other hand, can be found in some RNA molecules such as in the 3' untranslated region (UTR) of certain mRNAs or in specific types of non-coding RNAs like U-rich small nuclear RNAs (snRNAs).

Therefore, "Poly A-U" may refer to alternating sequences of adenine and uracil nucleotides in a DNA or RNA molecule. However, it is essential to consider the context in which this term is used to provide an accurate interpretation.

EC RNase A is an RNase that is commonly used in research. RNase A (e.g., bovine pancreatic ribonuclease A: PDB: 2AAS​ ... EC RNase V is specific for polyadenine and polyuridine RNA. EC RNase E is a ribonuclease of plant origin, ... EC number 3.1.??: RNase R is a close homolog of RNase II, but it can, unlike RNase II, degrade RNA with secondary structures ... RNase H leaves a 5-phosphorylated product. EC RNase III is a type of ribonuclease that cleaves rRNA (16s rRNA and ...
RNase, This group is composed of eukaryotic exoribonucleases that include PAN2, RNA exonuclease 1 (REX1 or Rex1p), REX3 (Rex3p ...
Learn about the sources of RNase contamination and how you can prevent them from disrupting your experiments. ... RNase activity can also be avoided by using RNase inhibitors, such as Murine RNase Inhibitor, which requires low concentration ... Use RNase-free solutions, and RNase-free certified, disposable plasticware and filter tips. Maintain a separate area for RNA ... Remove peroxide by extensively rinsing with RNase-free water prior to use. How can you prevent contamination during solution ...
52 kDa protein that is a potent non-competitive inhibitor of pancreatic-type ribonucleases such as RNase A, RNase B and RNase C ... RNase Inhibitor. RNase Inhibitor. For use in applications where the presence of RNases may pose a risk to RNA quality. ... The RNase Inhibitor is intended for molecular biology applications. This product is neither intended for the diagnosis, ... 20,000 U of RNAse Inhibitor (0.5 mL at 40,000 U/mL). Storage temperature: -25°C to -15°C ...
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RNase-free) is an endonuclease that nonspecifically cleaves DNA to release di-, tri- and oligonucleotide products with 5´- ... DNase I (RNase-free). M0303SVIAL. -20 1 x 0.5 ml 2,000 units/ml ... DNase I (RNase-free) GMP-grade reagent also available. Learn ... DNase I (RNase-free). M0303LVIAL. -20 2 x 1.25 ml 2,000 units/ml ... DNase I (RNase-free) is ideal for: *Removal of contaminating ... DNase I, (RNase-free) is an endonuclease that nonspecifically cleaves DNA to release di-, tri- and oligonucleotide products ...
Ribonuclease 6 (RNase 6) is one of eight catalytically active human pancreatic-type RNases that belong to a superfamily of ... Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.. Narayanan, C., Bernard, D.N. ... A comparison of the dynamical properties of RNase 6 in its apo-, substrate-, and product-bound states highlight the unique ... We present the first crystal structures of RNase 6 bound to a nucleotide ligand (adenosine 5-monophosphate), in addition to ...
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... and subsequently tested for inhibition of the enzymatic activity of ribonuclease A (RNase A). Reagent [PPN] 2 [ 1 ] reacts with ... and subsequently tested for inhibition of the enzymatic activity of ribonuclease A (RNase A) ... ... Nucleoside Tetra- and Pentaphosphates Prepared Using a Tetraphosphorylation Reagent Are Potent Inhibitors of Ribonuclease A.. ... We characterized inorganic and nucleoside-conjugated linear and cyclic oligophosphates as competitive inhibitors of RNase A. ...
Artificial Ribonucleases Authors. * Robert Häner Department of Chemistry and Biochemistry, University of Bern, Freiestr. 3, ... Artificial ribonucleases, Lanthanide complexes, Oligonucleotide, Rna, Rna cleavage Abstract. Chemically modified ... synthetic constructs of oligonucleotides and lanthanide complexes can serve as artificial ribonucleases. In this paper, some ... of modified oligonucleotides originating from our research efforts directed at the development of artificial ribonucleases are ...
Our study reveals a novel pathway of small guide RNA maturation and the first example of a host factor (RNase III) required for ... We show that tracrRNA directs the maturation of crRNAs by the activities of the widely conserved endogenous RNase III and the ... in which a trans-encoded small RNA directs processing of precursor RNA into crRNAs through endogenous RNase III and the CRISPR- ... pyogenes that employs trans-encoded small RNA that directs the processing of precursor RNA into crRNAs through endogenous RNase ...
RNase T2 is detected in all tissues in human, especially in immune cells. It includes both intracellular and secretory forms ... RNase T2 is highly conserved in mammals, which preferentially cleaves single-stranded RNA molecules between purine and uridine ... In this review, we introduce the distribution and expression pattern of RNase T2, its differential roles in inflammation and ... Accumulating studies have revealed that RNase T2 is critical for the pathophysiology of inflammation and cancer. In this review ...
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Most ribozymes cleave their own nucleotide sequence; however, Ribonuclease P can cleave other RNA molecules. Ribonuclease P is ... Bacterial Ribonuclease P is an RNA-protein complex that has endonuclease activity and requires Mg2+ ions. Its RNA component ... The type I and II introns and bacterial Ribonuclease P are large ribozymes. Small ribozymes are 30 to 150 nucleotides long. ...
Protein target information for Ribonuclease PH (Agrobacterium vitis S4). Find diseases associated with this biological target ...
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More info for Superfamily a.149.1: RNase III endonuclease catalytic domain. Timeline for Superfamily a.149.1: RNase III ... Superfamily a.149.1: RNase III endonuclease catalytic domain appears in SCOP 1.65. *Superfamily a.149.1: RNase III endonuclease ... Superfamily a.149.1: RNase III endonuclease catalytic domain first appeared in SCOP 1.59, called Superfamily a.149.1: RNase III ... Superfamily a.149.1: RNase III endonuclease catalytic domain was called Superfamily a.149.1: RNase III endonuclease domain in ...
More info for Family a.149.1.1: RNase III catalytic domain-like. Timeline for Family a.149.1.1: RNase III catalytic domain-like ... Superfamily a.149.1: RNase III domain-like [69065] (3 families) *. Family a.149.1.1: RNase III catalytic domain-like [69066] (2 ... Family a.149.1.1: RNase III catalytic domain-like first appeared in SCOP 1.59, called Family a.149.1.1: RNase III endonuclease ... Fold a.149: RNase III domain-like [69064] (1 superfamily). core: 5 helices; one helix is surrounded by the others. ...
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RNase H genes cause distinct impacts on RNA:DNA hybrid formation and mutagenesis genome-wide. Jeremy W. Schroeder, Rebecca L. ... RNase H genes cause distinct impacts on RNA:DNA hybrid formation and mutagenesis genome-wide ... RNase H genes cause distinct impacts on RNA:DNA hybrid formation and mutagenesis genome-wide ... RNase H genes cause distinct impacts on RNA:DNA hybrid formation and mutagenesis genome-wide ...
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  • RNase activity can also be avoided by using RNase inhibitors, such as Murine RNase Inhibitor, which requires low concentration of DTT (less than 1 millimolar) to maintain activity, making it ideal for reactions where low DTT concentration is required (like, real-time RT-PCR). (neb.com)
  • The RNase Inhibitor is intended for molecular biology applications. (qiagen.com)
  • 20,000 U of RNAse Inhibitor (0.5 mL at 40,000 U/mL). (qiagen.com)
  • Non-competitive inhibitor of pancreatic-type ribonucleases e.g. (qiagen.com)
  • RNase Inhibitor is an acidic, 52 kDa protein that is a potent non-competitive inhibitor of pancreatic-type ribonucleases such as RNase A, RNase B and RNase C. The enzyme is provided as a fusion of the porcine RNase Inhibitor gene with a proprietary 22.5 kDa protein tag. (qiagen.com)
  • Instructions for using RNase Inhibitor are provided in the corresponding kit protocol in the resources below. (qiagen.com)
  • Dilutions of the enzyme were made in 1X RNase Inhibitor Reaction Buffer and added to 1000 μL reactions containing 1mM cytidine 2',3'-cyclic monophosphate, 1μg RNase A in a 1X reaction buffer containing 100mM Tris-Acetate, 1mM EDTA, pH 6.5. (qiagen.com)
  • RNase Inhibitor is ideal for RNA-sensitive applications such as RT-qPCR as even a small amount of RNase can be detrimental to the final experimental outcome. (meridianbioscience.com)
  • A 2-fold serial dilution of HeLa cell total RNA (1 μg - 0.075 μg) was reverse transcribed in the presence (lanes 1 - 5) and in the absence (lanes 7 - 11) of RNase Inhibitor, followed by the amplification of a 1 kb fragment of the angiotensin II receptor gene under standard PCR conditions. (meridianbioscience.com)
  • There was no detectable difference in PCR product in the presence or absence of RNase Inhibitor, indicating that the addition of RNase Inhibitor does not interfere with the function of reverse transcriptase during cDNA synthesis. (meridianbioscience.com)
  • The glycerol-free formulation ensures the compatibility of RNase Inhibitor (Glycerol Free) to lyophilized formats. (meridianbioscience.com)
  • Why do I need a RNase inhibitor? (meridianbioscience.com)
  • Do I always need to use an RNase inhibitor in my RT reaction? (meridianbioscience.com)
  • Can RNase inhibitor be used at higher temperatures? (meridianbioscience.com)
  • No, RNase inhibitor is a protein and will be denatured at higher temperatures. (meridianbioscience.com)
  • SecurRIN™ Advanced RNase Inhibitor is a premium tool for RNA protection from degradation during enzymatic reactions, storage or extraction. (biogen.cz)
  • SecurRIN™ Advanced RNase Inhibitor is a 50 kDa non-covalent inhibitor of RNase A, RNase B, and RNase C binding them in a 1 to 1 ratio. (biogen.cz)
  • It is a recombinant protein derived from E. coli strain carrying human placenta RNase Inhibitor gene. (biogen.cz)
  • SecurRIN™ Advanced RNase Inhibitor does not inhibit RNAses H, 1, T1, T2 and S1 Nuclease. (biogen.cz)
  • 1 - 2 units of the RNase Inhibitor are typically enough for 1 microliter of RNA reaction. (biogen.cz)
  • Add SecurRIN™ Advanced RNase Inhibitor in to the cDNA synthesis reaction (~40 units for 20 µl reaction tube) as the first component. (biogen.cz)
  • In case high contamination with RNAses is suspected, use 2 µl of the RNase Inhibitor. (biogen.cz)
  • RNase inhibitor is a human placenta inhibitor, which works to inhibit RNase A, B and C activity by forming a tight, non-covalent 1:1 complex. (levprot.com)
  • RNaseBLK Ribonuclease Inhibitor is a high-affinity inhibitor that specifically targets common ribonucleases, including RNase A, B, and C. It is an essential enzyme for safeguarding RNA against potential RNase contamination, without interfering with polymerase activity in PCR/RT-PCR assays. (vitanavitech.com)
  • Compared to the high oxidation-sensitive human RNase inhibitor, RNaseBLK is a more robust version of the RNase inhibitor and has improved resistance to oxidation. (vitanavitech.com)
  • Learn about the sources of RNase contamination and how you can prevent them from disrupting your experiments. (neb.com)
  • This RNase contamination can often go unnoticed. (meridianbioscience.com)
  • Significant levels of ambient RNase contamination can occur in minutes. (phoseon.com)
  • Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes. (wikipedia.org)
  • one method of isolating it is to boil a crude cellular extract until all enzymes other than RNase A are denatured. (wikipedia.org)
  • Ribonuclease 6 (RNase 6) is one of eight catalytically active human pancreatic-type RNases that belong to a superfamily of rapidly evolving enzymes. (rcsb.org)
  • Ribonucleases (RNases) are RNA-processing or -degrading enzymes that hydrolyze phosphodiester bonds within RNA molecules ( 1 ). (frontiersin.org)
  • Meanwhile, DNase and RNase are enzymes that degrade DNA and RNA. (pharma-industry-review.com)
  • To determine the possible significance of in vivo or in vitro enzyme action in ribonucleoprotein systems, rat liver microsomes and ribonucleoprotein particles (RNP) prepared from them by deoxycholate treatment were incubated for 1 hour at 37°C. with crystalline pancreatic ribonuclease (RNase) or various RNase-free crystalline proteolytic enzymes. (rupress.org)
  • Some of the characteristics of this RNase activity were determined and the results with proteolytic enzymes interpreted in light of this activity. (rupress.org)
  • The enzymes of the ribonuclease (RNase) family possess identica l or similar active site residues and conserved fold architecture. (inrs.ca)
  • Meridian RNase Inhibitors are highly efficient inhibitors of a broad spectrum of eukaryotic RNases and shows no inhibition of polymerase or reverse transcriptase activity, so can be used in cDNA synthesis or one-step PCR or quantitative PCR reactions. (meridianbioscience.com)
  • Once sufficient data was acquired, an automated data analysis method was developed to measure the enzymatic reaction constant (k) which would be used to determine the polymer's percentage inhibition, a measure of the polymer's capability to reduce RNase A's native activity, the means of which were still uncertain. (rutgers.edu)
  • Early during virus entry , the initial interactions of the viral particle with the cell result in the inhibition of RNase L activity during the first hours of the infection . (bvsalud.org)
  • In bacteria RNase P is also responsible for the catalytic activity of holoenzymes, which consist of an apoenzyme that forms an active enzyme system by combination with a coenzyme and determines the specificity of this system for a substrate. (wikipedia.org)
  • Overall, our results confirm the specific evolutionary adaptation of RNase 6 relative to its unique catalytic and biological activities. (rcsb.org)
  • Even trace amounts of RNase have a big impact on RNA sequencing, due to its catalytic action. (phoseon.com)
  • RNase H is a non-specific endonuclease and catalyzes the cleavage of RNA via a hydrolytic mechanism, aided by an enzyme-bound divalent metal ion. (wikipedia.org)
  • tracrRNA directs pre-crRNA cleavage by RNase III in vitro . (nature.com)
  • Syndromic tumours result from acquisition of a somatic, second variant that typically affects DICER1's critical RNase IIIb cleavage domain. (bmj.com)
  • In this work, we describe the production and purification of two new immunoconjugates, based on RNase T1 and the fungal ribotoxin α-sarcin, with optimized properties for tumor treatment due to the inclusion of a furin cleavage site. (upm.es)
  • Pancreatic ribonuclease (RNase I) catalyzes cleavage of the phosphodiester bond between the 5'-ribose of a nucleotide and the phosphate group attached to the 3'-ribose of an adjacent pyrimidine nucleotide forming a 2',3'-cyclic phosphate which may then be hydrolyzed to the corresponding 3'-nucleoside phosphate. (p212121.com)
  • QIAGEN Ribonuclease A (RNase A) is endonuclease-free and quality-controlled for use in plasmid purification procedures for digestion of RNA. (qiagen.com)
  • DNase I, (RNase-free) is an endonuclease that nonspecifically cleaves DNA to release di-, tri- and oligonucleotide products with 5´-phosphorylated and 3´-hydroxylated ends (1,2). (neb.com)
  • Ribonucleases (RNases) are ubiquitous and can be introduced into experiments in many ways: for example co-purification during RNA isolation, carryover from bare hands and pipette tips. (meridianbioscience.com)
  • Meridian RNase Inhibitors are from a recombinant protein that inhibits different RNases (A, B, C) by binding non-covalently in a 1:1 ratio. (meridianbioscience.com)
  • Yes, to be on the safe side, we highly recommend the use of RNase inhibitors in all RT reactions, since RNases are nearly everywhere, and it is very easy to contaminate samples during RNA preparation and reaction setup. (meridianbioscience.com)
  • It is worth noting that all intracellular RNAs are protected from RNase activity by a number of strategies including 5' end capping, 3' end polyadenylation, formation of an RNA·RNA duplex, and folding within an RNA protein complex (ribonucleoprotein particle or RNP). (wikipedia.org)
  • RNase T2 includes both intracellular and secretory types ( 5 ). (frontiersin.org)
  • The intracellular RNase T2 is mainly localized in lysosomes, mitochondria, vacuoles, and other organelles. (frontiersin.org)
  • The intracellular distribution pattern suggests that RNase T2 may be involved in degrading exogenous or endogenous RNAs in lysosome and regulating mitochondrial RNA metabolism ( 6 - 8 ). (frontiersin.org)
  • A form of RNase P that is a protein and does not contain RNA has recently been discovered. (wikipedia.org)
  • With either microsomes or RNP, RNase (0.5 to 1.0 mg. per ml.) degraded from 75 to 95 per cent of the RNA, with little protein breakdown being apparent when microsomes were used but with significant protein degradation in the RNP. (rupress.org)
  • We characterized inorganic and nucleoside-conjugated linear and cyclic oligophosphates as competitive inhibitors of RNase A. Increasing the chain length in both linear and cyclic inorganic oligophosphates resulted in improved binding affinity. (rcsb.org)
  • RNase inhibitors are commonly used as a precautionary measure in enzymatic manipulations of RNA to inhibit and control for such contaminants. (meridianbioscience.com)
  • We offer two grades of RNase A, molecular biology grade and chromatically purified from Bovine pancreas. (p212121.com)
  • T o obtain better insights into the mechanism of ribonucleotyic activity we have modeled 7 human RN ases and bovine RNase A each with two different model substrates (ACAC and AUAU). (inrs.ca)
  • One unit is required to inhibit 5 ng of RNAse A by 50% (measuring the hydrolysis of cytidine 2′, 3′-cyclic monophosphate). (biogen.cz)
  • In this study, we determine the structural and conformational properties experienced by RNase 6 upon binding to substrate and product analogues. (rcsb.org)
  • A comparison of the dynamical properties of RNase 6 in its apo-, substrate-, and product-bound states highlight the unique dynamical properties experienced on time scales ranging from nano- to milliseconds. (rcsb.org)
  • Our study reveals a novel pathway of small guide RNA maturation and the first example of a host factor (RNase III) required for bacterial RNA-mediated immunity against invaders. (nature.com)
  • The type I and II introns and bacterial Ribonuclease P are large ribozymes. (jove.com)
  • The highly conserved bacterial YbeY RNase has structural similarities to the MID domain of AGOs. (biomedcentral.com)
  • RNase PhyM is sequence specific for single-stranded RNAs. (wikipedia.org)
  • EC RNase T1 is sequence specific for single-stranded RNAs. (wikipedia.org)
  • EC RNase A is an RNase that is commonly used in research. (wikipedia.org)
  • To date, the function of only one of the S-locus genes, the S-RNase gene, has been determined. (psu.edu)
  • The RNASEH2B gene provides instructions for making one part (subunit) of a group of proteins called the RNase H2 complex. (medlineplus.gov)
  • The RNASEH2B gene mutations that cause Aicardi-Goutières syndrome likely result in a dysfunctional RNase H2 complex. (medlineplus.gov)
  • We present the first crystal structures of RNase 6 bound to a nucleotide ligand (adenosine 5'-monophosphate), in addition to RNase 6 bound to phosphate ions. (rcsb.org)
  • Ribonuclease A, DNase & Protease Free Molecular Biology Grade. (p212121.com)
  • 3314-What is the concentration of RNase A sold separately? (qiagen.com)
  • The RNase T2 family are widely distributed in living organisms and highly conserved from viruses to mammals ( 1 ). (frontiersin.org)
  • EC RNase E is a ribonuclease of plant origin, which modulates SOS responses in bacteria, for a response to the stress of DNA damage by activation of the SOS mechanism by the RecA/LexA dependent signal transduction pathway that transcriptionally depresses a multiplicity of genes leading to transit arrest of cell division as well as initiation of DNA repair. (wikipedia.org)
  • Cosilencing the expression of VP3 and RNase L in infected cells yields viral infectious particles at levels similar to those obtained in control infected cells , where no genes were silenced, suggesting that the capping activity of VP3 is not essential for the formation of infectious viral particles . (bvsalud.org)
  • Initial characterization of isolates by RNase T1 oligonucleotide fingerprinting was inconclusive. (cdc.gov)
  • Later on, once viral proteins are synthesized, the phosphodiesterase activity of VP3 degrades the cellular 2'-5'-oligoadenylates, which are potent activators of RNase L, preventing its activation. (bvsalud.org)
  • Mutations in these histidine residues lead to the inactivation of RNase T2 both in vivo and in vitro ( Figure 1A ). (frontiersin.org)
  • GERBU's Proteinase K 20mg/ml Solution, free from DNase/RNase, with high enzyme activity of ≥800U/ml, offers reliability, purity, and outstanding performance for your research. (pharma-industry-review.com)
  • Feng S, Cao Z. Is the role of human RNase H2 restricted to its enzyme activity? (medlineplus.gov)
  • The RNase-Free DNase Set provides efficient on-column digestion of DNA during RNA purification from cells and tissues using RNeasy Kits and the QIAamp RNA Blood Mini Kit. (qiagen.com)
  • The RNeasy Midi/Maxi Handbook contains a protocol for the use of the RNase-Free DNase Set for on-column DNA digestion on RNeasy midi or maxi spin columns. (qiagen.com)
  • Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. (wikipedia.org)
  • It does not require any cofactors for its activity EC RNase H is a ribonuclease that cleaves the RNA in a DNA/RNA duplex to produce ssDNA. (wikipedia.org)
  • EC RNase III is a type of ribonuclease that cleaves rRNA (16s rRNA and 23s rRNA) from transcribed polycistronic RNA operon in prokaryotes. (wikipedia.org)
  • This particular phosphodiesterase cleaves the 2'-5'-phosphodiester bond of the oligoadenylates, antagonizing the OAS / RNase L pathway. (bvsalud.org)
  • Co-processing of tracrRNA and pre-crRNA requires both endogenous RNase III and Csn1 in vivo . (nature.com)
  • It also digests double-stranded RNA (dsRNA)-Dicer family of RNAse, cutting pre-miRNA (60-70bp long) at a specific site and transforming it in miRNA (22-30bp), that is actively involved in the regulation of transcription and mRNA life-time. (wikipedia.org)
  • Contaminants such as RNase A are difficult to irreversibly inactivate in the absence of harsh chemicals. (phoseon.com)
  • Complete inactivation of laboratory contaminants, including the hard-to-kill RNase A, can be accomplished by the KeyPro system in under five minutes and at fraction of the cost of traditional methods. (phoseon.com)
  • This GERBU Proteinase K solution is DNase/RNase-Free and does not contain any contaminants that could introduce them, ensuring its utmost purity and effectiveness. (pharma-industry-review.com)
  • This ready-to-use solution has the same specifications as the RNase supplied in all QIAGEN plasmid DNA purification kits. (qiagen.com)
  • The QIAGEN RNase-Free DNase Set is guaranteed RNase-free, quality-controlled, and optimized for use with RNeasy procedures and with QIAamp RNA Blood Mini procedures. (qiagen.com)
  • The QIAGEN RNase-Free DNase Set is delivered as a stable, lyophilized enzyme. (qiagen.com)
  • This enzyme is detected in all tissues, especially in embryonic tissues and immune cells ( https://www.proteinatlas.org/ ) ( Figures 1B,C ). The full-length human RNase T2 has 256 amino acids (AA) and a predicted size of 29 kD ( Table 1 ). (frontiersin.org)
  • RNase A (17500 U), catalog number 19101, is 100mg/ml. (qiagen.com)
  • RNase A Solution (650 µl), catalog number 158922, and RNase A Solution (5 ml), catalog number 158924, are both 4mg/ml. (qiagen.com)
  • Description Ribonuclease A (RNase A) is an abundant nucleic acid metabolic enzyme found in almost every eukaryotic and prokaryotic cell type that catalyzes the breakdown of RNA molecules. (rutgers.edu)
  • the dissociation constant for the RI-RNase A complex is ~20 fM under physiological conditions. (wikipedia.org)
  • This complex is a ribonuclease, which means it is an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA. (medlineplus.gov)
  • In particular, the RNase H2 complex normally helps break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed. (medlineplus.gov)
  • The RNase H2 complex is also thought to be involved in DNA replication, error repair, and other cellular processes, including helping to prevent inappropriate immune system activation. (medlineplus.gov)
  • Contributions of the two accessory subunits, RNASEH2B and RNASEH2C, to the activity and properties of the human RNase H2 complex. (medlineplus.gov)
  • Use RNase-free solutions, and RNase-free certified, disposable plasticware and filter tips. (neb.com)
  • Remove peroxide by extensively rinsing with RNase-free water prior to use. (neb.com)
  • The RNase-Free DNase Set provides 1500 Kunitz units. (qiagen.com)
  • Available with foam, flocked, or cotton tips, our DNA-free and RNase-free sampling swabs have been tested by an independent lab to the most stringent standards. (puritanmedproducts.com)
  • Proteinase K Solution - DNase/RNase-Free is a liquid form of Proteinase K that has been purified and tested for the absence of DNase and RNase. (pharma-industry-review.com)
  • Therefore, it is important to use solutions that are free of DNase and RNase when working with DNA or RNA. (pharma-industry-review.com)
  • The volume of RNAse free water to use in the QIAcube depends on the number of samples to process. (lu.se)
  • Many stress-response toxins of prokaryotic toxin-antitoxin systems have been shown to have RNase activity and homology. (wikipedia.org)
  • Ribonuclease A has a molecular weight of 13,700 daltons and has optimum activity in a pH range of 7.0-7.5. (p212121.com)
  • Both microsomes and RNP contained significant RNase activity with RNP exhibiting about 10 times the specific activity of microsomes. (rupress.org)
  • This work demonstrates that the OAS / RNase L pathway plays an important role during infection and that the phosphodiesterase activity of VP3 is relevant during the replication cycle of the virus . (bvsalud.org)
  • The evolutionary conservation structure of RNase T2 and distribution of RNASET2 in human tissues and immune cells. (frontiersin.org)
  • The Solanaceae, Rosaceae, and Scrophulariaceae families all possess an RNase-mediated self-incompatibility mechanism through which their pistils can recognize and reject self-pollen to prevent inbreeding. (psu.edu)
  • however, Ribonuclease P can cleave other RNA molecules. (jove.com)
  • This Proteinase K solution has been purified and tested for the absence of DNase and RNase and is ideally suitable for DNA and RNA extraction applications. (pharma-industry-review.com)
  • The RNase T2 family consists of evolutionarily conserved endonucleases that express in many different species, including animals, plants, protozoans, bacteria, and viruses. (frontiersin.org)
  • All RNase T2 family members exhibit a conserved α/β core structure. (frontiersin.org)
  • In human, RNase T2 is the only identified member of the RNase T2 family ( 4 ). (frontiersin.org)
  • Using theoretical modeling and atomistic molecular simulations at mic rosecond time scale, we are investigating the role of functionally important conformational sub-states in relation to optimal catalysis by the members of the pancreatic RNase enzyme family. (inrs.ca)
  • Like some of its human homologues, RNase 6 exhibits host defense properties such as antiviral and antibacterial activities. (rcsb.org)
  • Human RNase T2 shows a typical structure, containing seven α-helices and eight β-strands. (frontiersin.org)
  • Ribonuclease P is found in some bacteria and processes precursor tRNA to generate a mature 5' end. (jove.com)