Amino Acids: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Amino Acid Sequence: 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.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Cloning, Molecular: 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.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Sequence Alignment: 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.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Escherichia coli: 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.Mutation: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Amino Acids, Aromatic: Amino acids containing an aromatic side chain.Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Molecular Sequence Data: 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.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Amino Acids, SulfurKinetics: The rate dynamics in chemical or physical systems.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Protein Conformation: 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).Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Structure-Activity Relationship: 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.Protein Structure, Tertiary: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.DNA: 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).Molecular Weight: The sum of the weight of all the atoms in a molecule.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Protein Binding: 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.Bacterial Proteins: Proteins found in any species of bacterium.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Genes, Bacterial: The functional hereditary units of BACTERIA.Proteins: 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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.RNA, Messenger: 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.Amino Acid Transport Systems, Basic: Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).Protein Structure, Secondary: 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.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Isoleucine: An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.Amino Acids, Basic: Amino acids with side chains that are positively charged at physiological pH.Lysine: An essential amino acid. It is often added to animal feed.Species Specificity: The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Codon: A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).Cyanogen Bromide: Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.Trypsin: 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 3.4.21.4.Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.Cattle: 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.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Amino Acids, DiaminoGlutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.Open Reading Frames: A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.Valine: A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Excitatory Amino Acids: Endogenous amino acids released by neurons as excitatory neurotransmitters. Glutamic acid is the most common excitatory neurotransmitter in the brain. Aspartic acid has been regarded as an excitatory transmitter for many years, but the extent of its role as a transmitter is unclear.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Arginine: An essential amino acid that is physiologically active in the L-form.Aspartic Acid: One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.Gene Library: A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Sequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Sequence Analysis: A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.Proline: A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Point Mutation: A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Amino Acid Transport System A: A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.Amino Acids, Neutral: Amino acids with uncharged R groups or side chains.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Tryptophan: An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Blotting, Northern: Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Viral Proteins: Proteins found in any species of virus.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.Receptors, Amino Acid: Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Epitopes: Sites on an antigen that interact with specific antibodies.Dietary Proteins: Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Swine: Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).Protein PrecursorsCOS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Chymotrypsin: 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.Protein Sorting Signals: Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.Amino Acids, Cyclic: A class of amino acids characterized by a closed ring structure.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Chromatography, Ion Exchange: 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.Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.Repetitive Sequences, Amino Acid: A sequential pattern of amino acids occurring more than once in the same protein sequence.DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Aminoisobutyric Acids: A group of compounds that are derivatives of the amino acid 2-amino-2-methylpropanoic acid.Chickens: Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.Fungal Proteins: Proteins found in any species of fungus.DNA Mutational Analysis: Biochemical identification of mutational changes in a nucleotide sequence.Glutamic Acid: A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.Blotting, Southern: A method (first developed by E.M. Southern) for detection of DNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.Temperature: 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.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Chromosome Mapping: Any method used for determining the location of and relative distances between genes on a chromosome.Circular Dichroism: 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)Large Neutral Amino Acid-Transporter 1: A CD98 antigen light chain that when heterodimerized with CD98 antigen heavy chain (ANTIGENS, CD98 HEAVY CHAIN) forms a protein that mediates sodium-independent L-type amino acid transport.Enzyme Stability: 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.Genetic Variation: Genotypic differences observed among individuals in a population.Oligopeptides: Peptides composed of between two and twelve amino acids.Genes, Fungal: The functional hereditary units of FUNGI.Hydrogen-Ion Concentration: 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)Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Oligonucleotide Probes: Synthetic or natural oligonucleotides used in hybridization studies in order to identify and study specific nucleic acid fragments, e.g., DNA segments near or within a specific gene locus or gene. The probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the probe include the radioisotope labels 32P and 125I and the chemical label biotin.Cystine: A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.Amino Acids, Acidic: Amino acids with side chains that are negatively charged at physiological pH.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Exons: The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA.Oligodeoxyribonucleotides: A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.Sequence Homology: The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.Genetic Code: The meaning ascribed to the BASE SEQUENCE with respect to how it is translated into AMINO ACID SEQUENCE. The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (CODON).Asparagine: A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Carbohydrates: The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.Magnetic Resonance Spectroscopy: 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).Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Culture Media: Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.Caseins: A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Mutation, Missense: A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)Tissue Distribution: Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Cercopithecus aethiops: A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Genes, Viral: The functional hereditary units of VIRUSES.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Consensus Sequence: A theoretical representative nucleotide or amino acid sequence in which each nucleotide or amino acid is the one which occurs most frequently at that site in the different sequences which occur in nature. The phrase also refers to an actual sequence which approximates the theoretical consensus. A known CONSERVED SEQUENCE set is represented by a consensus sequence. Commonly observed supersecondary protein structures (AMINO ACID MOTIFS) are often formed by conserved sequences.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.RNA: 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)Histidine: An essential amino acid that is required for the production of HISTAMINE.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.DNA Restriction Enzymes: Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1.Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Xenopus laevis: The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Transaminases: A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.Cationic Amino Acid Transporter 1: A high-affinity, low capacity system y+ amino acid transporter found ubiquitously. It has specificity for the transport of ARGININE; LYSINE; and ORNITHINE. It may also act as an ecotropic leukemia retroviral receptor.Amino Acid Isomerases: Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.Binding, Competitive: The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Protein Engineering: Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.Nucleic Acid Hybridization: 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)Membrane Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.Dipeptides: Peptides composed of two amino acid units.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Biological Transport, Active: The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.Solubility: The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Biological Evolution: The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.

Twelfth rib resection as an approach for portal vein cannulation in sheep. (1/23787)

A surgical technique involving resection of the twelfth rib was used to insert silastic cannulas into the portal veins of three sheep to study amino acid metabolism. Good exposure to the vein was achieved by this method although it required positive ventilation due to the penetration of the thoracic cavity. All cannulas were buried subcutaneously and exteriorized near the dorsal midline. This facilitated continuous infusion into the portal cannula without disturbing cannula placement.  (+info)

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides. (2/23787)

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem J. (1975) 145, 5.  (+info)

The isolation and partial characterization of the serum lipoproteins and apolipoproteins of the rainbow trout. (3/23787)

1. VLD (very-low-density), LD (low-density) and HD (high-density) lipoproteins were isolated from the serum of trout (Salmo gairdneri Richardson). 2. Each lipoprotein class resembled that of the human in immunological reactivity, electrophoretic behaviour and appearance in the electron microscope. Trout LD lipoprotein, however, was of greater density than human LD lipoprotein. 3. The trout lipoproteins have lipid compositions which are similar to those of the corresponding human components, except for their high contents of long-chain unsaturated fatty acids. 4. HD and LD lipoproteins were immunologically non-identical, whereas LD lipoproteins possessed antigenic determinants in common with VLD lipoproteins. 5. VLD and HD lipoproteins each contained at least seven different apoproteins, whereas LD liprotein was composed largely of a single apoprotein which resembled human apolipoprotein B. 6. At least one, and possibly three, apoprotein of trout HD lipoprotein showed features which resemble human apoprotein A-1.7. The broad similarity between the trout and human lipoprotein systems suggests that both arose from common ancestral genes early in evolutionary history.  (+info)

Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C-terminal regions of the protein. (4/23787)

1. Trypsin digestion of human serum transferrin partially saturated with iron(III)-nitrilotriacetate at pH 5.5 or pH 8.5 produces a carbohydrate-containing iron-binding fragment of mol.wt. 43000. 2. When iron(III) citrate, FeCl3, iron (III) ascorabate and (NH4)2SO4,FeSO4 are used as iron donors to saturate the protein partially, at pH8.5, proteolytic digestion yields a fragment of mol.wt. 36000 that lacks carbohydrate. 3. The two fragments differ in their antigenic structures, amino acid compositions and peptide 'maps'. 4. The fragment with mol.wt. 36000 was assigned to the N-terminal region of the protein and the other to the C-terminal region. 5. The distribution of iron in human serum transferrin partially saturated with various iron donors was examined by electrophoresis in urea/polyacrylamide gels and the two possible monoferric forms were unequivocally identified. 6. The site designated A on human serum transferrin [Harris (1977) Biochemistry 16, 560--564] was assigned to the C-terminal region of the protein and the B site to the N-terminal region. 7. The distribution of iron on transferrin in human plasma was determined.  (+info)

Salivary mucin MG1 is comprised almost entirely of different glycosylated forms of the MUC5B gene product. (5/23787)

The MG1 population of mucins was isolated from human whole salivas by gel chromatography followed by isopycnic density gradient centrifugation. The reduced and alkylated MG1 mucins, separated by anion exchange chromatography, were of similar size (radius of gyration 55-64 nm) and molecular weight (2.5-2.9 x 10(6) Da). Two differently-charged populations of MG1 subunits were observed which showed different reactivity with monoclonal antibodies to glycan epitopes. Monosaccharide and amino acid compositional analyses indicated that the MG1 subunits had similar glycan structures on the same polypeptide. An antiserum recognizing the MUC5B mucin was reactive across the entire distribution, whereas antisera raised against the MUC2 and MUC5AC mucins showed no reactivity. Western blots of agarose gel electrophoresis of fractions across the anion exchange distribution indicated that the polypeptide underlying the mucins was the product of the MUC5B gene. Amino acid analysis and peptide mapping performed on the fragments produced by trypsin digestion of the two MG1 populations yielded data similar to that obtained for MUC5B mucin subunits prepared from respiratory mucus (Thornton et al., 1997) and confirmed that the MUC5B gene product was the predominant mucin polypeptide present. Isolation of the MG1 mucins from the secretions of the individual salivary glands (palatal, sublingual, and submandibular) indicate that the palatal gland is the source of the highly charged population of the MUC5B mucin.  (+info)

Association of polymorphism at the type I collagen (COL1A1) locus with reduced bone mineral density, increased fracture risk, and increased collagen turnover. (6/23787)

OBJECTIVE: To examine the relationship between a common polymorphism within intron 1 of the COL1A1 gene and osteoporosis in a nested case-control study. METHODS: We studied 185 healthy women (mean +/- SD age 54.3+/-4.6 years). Bone mineral density (BMD) was measured using dual x-ray absorptiometry, and fractures were determined radiographically. The COL1A1 genotype was assessed using the polymerase chain reaction and Bal I endonuclease digestion. RESULTS: Genotype frequencies were similar to those previously observed and in Hardy-Weinberg equilibrium: SS 61.1%, Ss 36.2%, and ss 2.7%. Carriage of at least one copy of the "s" allele was associated with a significant reduction in lumbar spine BMD (P = 0.02) and an increased risk of total fracture (P = 0.04). Urinary pyridinoline levels were significantly elevated in those with the risk allele (P < 0.05). CONCLUSION: These data support the findings that the COL1A1 gene polymorphism is associated with low BMD and fracture risk, and suggest a possible physiologic effect on total body turnover of type I collagen.  (+info)

Basic homopolyamino acids, histones and protamines are potent antagonists of angiogenin binding to ribonuclease inhibitor. (7/23787)

A radio-ribonuclease inhibitor assay based on the interaction of 125I-angiogenin with ribonuclease inhibitor (RI) was used to detect pancreatic-type ribonucleases and potential modulators of their action. We show that highly basic proteins including the homopolypeptides poly-arginine, poly-lysine and poly-ornithine, core histones, spermatid-specific S1 protein and the protamines HP3 and Z3 were strong inhibitors of angiogenin binding to RI. A minimum size of poly-arginine and poly-lysine was required for efficient inhibition. The inhibition likely resulted from direct association of the basic proteins with the acidic inhibitor, as RI bound to poly-lysine and protamines while 125I-angiogenin did not. Antagonists of the angiogenin-RI interaction are potential regulators of either angiogenin-triggered angiogenesis and/or intracellular RI function, depending on their preferential target.  (+info)

The DNA binding activity of Translin is mediated by a basic region in the ring-shaped structure conserved in evolution. (8/23787)

DNA binding proteins, for the most part, function as dimers or tetramers which recognize their target sequences. Here we show that Translin, a novel single-stranded DNA end binding protein, forms a ring-shaped structure conserved throughout evolution and that this structure is responsible for its DNA binding activity. Point mutations at Leu184 and Leu191 in the leucine zipper motif of human Translin resulted in loss of the multimeric structure and abrogation of DNA binding. Point mutations at R86, H88, H90 to T86, N88, N90 in one of the basic regions, however, completely inhibited the DNA binding activity without affecting the multimeric structure. These results support the view that the DNA binding domain of Translin is formed in the ring-shaped structure in combination with its basic region (amino acids 86-97) polypeptides.  (+info)

Table of Contents of Amino Acid Analyzer Market:. 1 Study Coverage. 1.1 Amino Acid Analyzer Product. 1.2 Key Market Segments in This Study. 1.3 Key Manufacturers Covered. 1.4 Market by Type. 1.5 Market by Application. 2 Executive Summary. 2.1 Global Amino Acid Analyzer Production. 2.2 Amino Acid Analyzer Growth Rate (CAGR) 2018-2024. 2.3 Analysis of Competitive Landscape. 2.4 Market Drivers, Trends and Issues. 2.5 Macroscopic Indicator. Purchase This Report (Price 3480 USD for single user license): https://www.absolutereports.com/purchase/13837546. 4 Amino Acid Analyzer Production by Regions. 4.1 United States. 4.2 Europe. 4.3 China. 4.4 Japan. 4.5 Other Regions. 6 Market Size by Type. 6.1 Global Amino Acid Analyzer Breakdown Data by Type. 6.2 Global Amino Acid Analyzer Revenue by Type. 6.3 Amino Acid Analyzer Price by Type. 7 Market Size by Application. 7.1 Overview. 7.2 Global Amino Acid Analyzer Breakdown Data by Application. 7.2.1 Global Amino Acid Analyzer Consumption by Application. 7.2.2 ...
Proteinogenic amino acids, also known as standard, normal, or primary amino acids, are those 20 amino acids that are found in proteins and that are coded for in the standard genetic code. Proteinogenic literally means protein building. Proteinogenic amino acids are assembled into a polypeptide (the subunit of a protein) through a process known as translation (the second stage of protein biosynthesis, part of the overall process of gene expression). Non-proteinogenic amino acids are either not found in proteins (like carnitine, GABA, or L-DOPA), or not coded for in the standard genetic code (like hydroxyproline and selenomethionine). The latter often result from posttranslational modification of proteins. Some non-proteinogenic amino acids, such as ornithine and homoserine have clear reasons why organisms have not evolved to incorporate them into proteins; both of these amino acids will cyclize against the peptide backbone and fragment the protein with relatively short half-lives. Some ...
How much of Glutamic acid, Glu or E, proteinogenic amino acid is present in Pork, fresh, loin, whole, separable lean only, cooked, braised in details, quantity how high or low Glutamic acid, Glu or E, proteinogenic amino acid nutrient content it has.
How much of Serine, Ser or S, proteinogenic amino acid is present in Rice noodles, dry in details, quantity how high or low Serine, Ser or S, proteinogenic amino acid nutrient content it has.
Unfortunately, this study leaves us with way more questions than answers. I personally, for example would venture the guess that the ingestion of a complete EAA product would result in an even more profound amelioration of the fasting induced reduction in fractional protein synthesis. That being said, the latter could also compromise another advantage of the non-essential amino acids, I have not even mentioned, yet: their almost non-existent effect on intra-muscular AMPK-expression (cf. figure 2, right). If you read all Intermittent Thoughts articles which dealt with the AMPK/mTOR Metabolic Seesaw and the respective follow-ups, you will be familiar with notion that the fasting-induced phosphorylation of intra-muscular AMPK is responsible for the majority of the health, as well as the closely related fat-burning effects of (intermittent) fasting. Now, if the ingestion of a ~20g bolus of alanine, glycine, proline, histidine, asparagine and serine could increase your skeletal muscle protein ...
It is not quite clear so far to what extent the requirement for total non-essential N can be influenced by the presence or absence of different non-essential amino acids. There are a number of studies indicating that some amino acids, commonly classified as non-essential, may have essential character (Breuer et al., 1964; Newburg et al., 1975; Ball et al., 1986; Roth et al, 1994a) whereas some others are inferior as sources of non-specific N (Sugahara and Ariyoshi, 1967b; Allen and Baker, 1974). Therefore, both the specific requirements for non-essential amino acids and the value of these amino acids in supplying the organism with non-specific nitrogen should be taken into account when studying the optimum E:T ratio and formulating amino acid diets.. Results of studies aimed at identification of non-essential amino acids needed for normal performance have been controversial. The requirement for proline has been demonstrated in rats (Breuer et al., 1964; Heger et al., 1987), chicks (Sugahara and ...
Can you name the Essential and Non-Essential Amino Acids? Test your knowledge on this science quiz to see how you do and compare your score to others. Quiz by Gaijindesu
TY - JOUR. T1 - Serum amino acids following human orthotopic liver transplantation. AU - Munoz, S. J.. AU - Jarrell, B. E.. AU - Westerberg, S.. AU - Miller, L.. AU - Moritz, M. J.. AU - Maddrey, W. C.. PY - 1993/1/1. Y1 - 1993/1/1. UR - http://www.scopus.com/inward/record.url?scp=0027252837&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0027252837&partnerID=8YFLogxK. M3 - Article. C2 - 8470162. AN - SCOPUS:0027252837. VL - 25. SP - 1779. EP - 1782. JO - Transplantation Proceedings. JF - Transplantation Proceedings. SN - 0041-1345. IS - 2. ER - ...
Before going ahead and understanding proteins - the biomolecules, it is important to first understand amino acids. Amino acids are the organic compounds mainly bonded to a hydrogen atom, a carboxyl group (COO-) and an amine group (NH2) along with a side chain (represented as R in the diagram) which is specific to every amino acid. There are about 500 amino acids known. The two broad groups into which these amino acids can be distributed are: proteinogenic amino acids and non-proteinogenic amino acids. The word proteinogenic means protein building. Interesting to note is that of these 500 amino acids, only 23 naturally occurring amino acids come under proteinogenic amino acids i.e.; these amino acids are precursors to proteins. Of these 23, 20 proteinogenic amino acids are encoded by codons (triplet) in genetic code and are called standard amino acids. The other three which are non-standard amino acids are pyrrolysine, selenocysteine and N-formylmethionine. The pyrrolysine is found in ...
解釋 Cysteine (L-cysteine, Cys, C) proteinogenic amino acid molecule. Structural chemical formula and molecule model. Vector illustration 剪貼畫、和美工 Image 124098273.
1. After ingestion of up to 1-2 g of protein/kg body weight by adults, plasma concentrations of all amino acids, including glutamine and glutamic acid, rose to a maximum within 5 h.. 2. The increases in concentration depended on the amount of protein ingested.. 3. The changes were not due to diurnal variation in plasma amino acid levels, so, protein loading tests may be of value in the assessment of protein absorption. ...
Mass spectrometry-based serum metabolic profiling is a promising tool to analyse complex cancer associated metabolic alterations, which may broaden our pathophysiological understanding of the disease and may function as a source of new cancer-associated biomarkers. Highly standardized serum samples of patients suffering from colon cancer (n = 59) and controls (n = 58) were collected at the University Hospital Leipzig. We based our investigations on amino acid screening profiles using electrospray tandem-mass spectrometry. Metabolic profiles were evaluated using the Analyst 1.4.2 software. General, comparative and equivalence statistics were performed by R 2.12.2. 11 out of 26 serum amino acid concentrations were significantly different between colorectal cancer patients and healthy controls. We found a model including CEA, glycine, and tyrosine as best discriminating and superior to CEA alone with an AUROC of 0.878 (95% CI 0.815-0.941). Our serum metabolic profiling in colon cancer revealed ...
The α-ketoglutarate family of amino acid synthesis (synthesis of glutamate, glutamine, proline and arginine) begins with α-ketoglutarate, an intermediate in the Citric Acid Cycle. The concentration of α-ketoglutarate is dependent on the activity and metabolism within the cell along with the regulation of enzymatic activity. In E. coli citrate synthase, the enzyme involved in the condensation reaction initiating the Citric Acid Cycle is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP.[5] This is one of the initial regulations of the α-ketoglutarate family of amino acid synthesis. The regulation of the synthesis of glutamate from α-ketoglutarate is subject to regulatory control of the Citric Acid Cycle as well as mass action dependent on the concentrations of reactants involved due to the reversible nature of the transamination and glutamate dehydrogenase reactions.[5] The conversion of glutamate to glutamine is ...
With reductions in crude protein (CP) levels and higher supplementation of crystalline essential amino acids (EAA) in swine diets, the supply of non-essential amino acids (NEAA), or nitrogen (N) required for the synthesis of NEAA, is also reduced increasing the ratio between EAA-N and total N in the diet. When diets are deficient in NEAA-N, non-protein N (NPN) could supply additional N required for the endogenous synthesis of NEAA. The main objective of the present thesis was to assess the efficiency of ammonia for providing extra N when diets are deficient in NEAA-N. Secondary objectives were to determine the effects of ammonia supplementation on the amino acid (AA) profile of retained protein as an indicator of AA requirements and quantification of ammonia absorption and metabolism in the portal-drained viscera (PDV) and liver. Added ammonia to a NEAA-N deficient diet increased body weight (BW) gain and N retention and rendered similar efficiencies as supplemented Glu and a mix of NEAA ...
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Serum amino acid profiling reveals a pattern of disturbed urea cycle function in Addisons patients. Amino acid (A) arginine (ARG), ornithine (ORN) and citrulli
L-Arginine was discovered back in 1886. It reportedly came from the extract of a lowly bean. Arginine is an amino acid that can be made in the human body, otherwise known as a non-essential amino acid. A non-essential amino acid is called "non-essential" because it is one that can be made by the human body and so is not essential to the human diet. There are 11 nonessential amino acids: arginine, alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine. There are also essential amino acids. These are amino acids that cannot be made by the body. As a result, they must come from food.. Arginine is commonly found in many protein-rich foods. A few arginine-rich foods include steak, turkey, chicken, pork, pumpkin seeds and soy products. In researching this article I also found out on www.nutritiondata.self.com, that sea lion is incredibly high in arginine, but unless your an Eskimo, I doubt thats an actual menu choice. The average American diet ...
Package Labelling for Amino Acids: The United States Food & Drug Administration (USFDA) as per its directive [21 CFR 101.36(b)(2)(i)] stipulates that a dietary supplement containing amino acids must be labelled as such and the amino acid profile should be clearly displayed on the display panel of the package. Moreover, it should not be labeled as a protein if only amino acids are present.. How is the Amino Acid Profile Determined?. Determination of the amino acid profile of proteins and peptides present in many types of samples, including food samples like dietary supplements, is a fundamental biochemical technique. The number of free amino acids, as well as amino acids released from proteins and peptides, can be quantitated by the procedure of amino acid analysis. Generally, UV spectrophotometry and high-pressure liquid chromatography (HPLC) are used for determination of the amino acid profile of samples. This is done following good laboratory practices (GLP) in specialized laboratories with ...
Amino Acids play an important role in better nutrition and a healthier body. Browse the extensive iHerb selection of natural amino acid supplements.
Amino Acids play an important role in better nutrition and a healthier body. Browse the extensive iHerb selection of natural amino acid supplements.
Amino Acids play an important role in better nutrition and a healthier body. Browse the extensive iHerb selection of natural amino acid supplements.
Amino acids are classified into two groups, essential and non-essential amino acids. Essential amino acids (BCAA, branched chained amino acids) means the body cannot naturally produce these acids but are typically found in nutritional supplements or in the foods we eat. Non-essential amino acids are acids that are naturally produced by the body(hormones from thyroid…
Researchers tested a new amino acid supplement energy bar enriched with L-leucine to investigate if this could improve protein and energy intake in older women.
Our body does not come with a guarantee. Just because we are designed to synthesize and metabolize non-essential amino acids, does not mean everyone is able to. Every system, no matter how well designed can suffer from flaws, and human body is not an exception. Metabolic flaws have major impact on how our body uses nutrients and facilitates the function of cells, tissues and organs. They are dispersed with lottery like odds. But instead of winning thousands of dollars, metabolic lottery costs the sufferers thousands of dollars in therapies that help them live until the cure is found.. There are unlucky few born with major errors in non-essential amino acid metabolism. There are no rules. That can be our mother, sister, father, child, a neighbor, stranger crossing a street, anyone. And while we enjoy our steaks, live, run, laugh and take our health for granted, they have to struggle every day to survive. And they would give anything to switch places.. So what prevents them? The inborn pre-exiting ...
If youve been following along then by now youve figured out that science has proven that even less than half a gram of protein per pound of bodyweight per day is enough to both retain and build muscle mass. Today Id like to look into amino acids to see what we can learn and also to see if I can wrap this series up.. Obviously, the important component of the protein seems to be the essential amino acid content. It is now clear that muscle anabolism occurs with ingestion of only the essential amino acids meaning the non-essential amino acids are unnecessary to stimulate muscle growth following exercise(1). However, this doesnt mean that essential amino acid supplements are superior to non-essential or to whole proteins. It simply means that essential amino acids can stimulate muscle protein synthesis and there are ample non-essentials to support the elevated levels of synthesis.. Leucine may be the most important amino acid for stimulation of muscle protein synthesis. Leucine, along with ...
Amino acids can be classified according to various structural and functional properties. The classification into proteinogenic and non-proteinogenic amino acids is of essential importance in the life sciences. The former are structurally characterized by having a C-α-atom which is bound to a carboxy group, an amino group and an organic side chain R. In total, 22 different proteinogenic amino acids are known, including selenocysteine and pyrrolysine. While selenocysteine (Sec) occurs in different eukaryotic enzymes, for example in glutathione peroxidase, pyrrolysine (N6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl-carbonyl]-L-lysine) was only found in methanogenic bacteria as yet. 21 of the 22 proteinogenic amino acids are chiral with the exception of glycine where the side chain is substituted by an H atom. Accordingly, members of the former group can exist in two enantiomeric forms referred to as L- and D-isomers. The D-configuration, for example, is found in bacterial cell walls while in ...
Amino acid synthesis is the process of creating new amino acids inside an organisms cells for the body to use to make proteins...
The 20 amino acids involved in protein biosynthesis are divided into two broad groups, essential and non-essential. For good health, eight of these amino acids are essential and must be taken either in the form of pill or capsule, in addition to the minuscule amounts found in the food we eat. The remaining 12 non-essential amino acids,the body can synthesize from the diet. For example, Betamine is a non-essential amino acid. It is found in beetroot. When the tuber is included in the diet, the body uses the Betamine in it for the production of Dopamine. People suffering from Parkinson and those who are not, are advised to include beetroot frequently in the diet.. ...
Excess alcohol consumption is a top risk factor for death and disability. Fatty liver will likely develop and the risk of liver disease increases. We have previously demonstrated that an essential amino acid supplement (EAAS) improved protein synthesis and reduced intrahepatic lipid in the elderly. The purpose of this study was to further evaluate the influence of EAAS on intrahepatic lipid (IHL), body composition, and blood lipids in individuals with mild to moderate alcohol use disorder (AUD). Following consent, determination of eligibility, and medical screening, 25 participants (18 males at 38±15 years/age and 7 females at 34±18 years/age) were enrolled and randomly assigned to one of two dosages: a low dose (LD: 8 grams of EAAS twice/day (BID)) or high dose (HD: 13 grams of EAAS BID). Both groups consumed the supplement for 4 weeks. Pre- and post-EAAS administration, IHL was determined using magnetic resonance imaging/spectroscopy, body composition was analyzed using dual energy x-ray
L-Glutamine L-Glutamine is a non-essential Amino Acid that is produced by the body but can also be found in food. The human body requires about 20 essential and non-essential Amino Acids to create and utilize enough protein for the body to function adequately. When the body is in a stressed state (e.g. during exercise)
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1. The incorporation into protein, and the accumulation into the free amino acid pools, of radioactive l-leucine and glycine was studied in rat extensor digitorum longus muscle. 2. The tissue was incubated first with 14C-labelled and then with 3H-labelled amino acid. 3. The experimental results were consistent with a model based on the premise that the amino acids in protein were incorporated directly from the extracellular pool.. ...
Arginine is considered The Natural Viagra by increasing blood flow to the penis; retards the growth of tumors and cancer by enhancing the immune system
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Amino acids are the building blocks of protein. Amino acids & amino acid supplements are of critical importance and are considered among the most important supplements. They can aid in muscle repair, muscle recovery & support lean muscle growth.
View Notes - Lecture 13 amino acid synthesis from BIOLCHEM 415 at University of Michigan. BergTymoczkoStryer Biochemistry Chapter24: TheBiosynthesisofAminoAcids CopyrightbyW.H.FreemanandCompany Overvi
Because of increased incidence of teenage births and high prevalence of lactation in Latin America, we determined the patterning of free amino acids (FAAs) in breast milk of 65 primiparous Ecuadorian women of varying ages (14-27 years). An automatic amino acid analyzer quantified levels of FAAs in milk samples obtained at three lactation stages: colostrum, transition, and mature milk. Regardless of mothers age, most FAAs increased with time postpartum, with taurine, glutamic acid, glutamine, and alanine being most abundant in all stages.
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Amino acids[edit]. BMAA[edit]. The non-proteinogenic amino acid beta-Methylamino-L-alanine (BMAA) is ubiquitously produced by ... Amino Acid BMAA Nervous System All Most cyanotoxins have a number of variants (analogues). As of 1999, altogether over 84 ... A peptide is a short polymer of amino acids linked by peptide bonds. They have the same chemical structure as proteins, except ... a neurotoxic amino acid". PNAS. 102 (14): 5074-5078. Bibcode:2005PNAS..102.5074C. doi:10.1073/pnas.0501526102. PMC 555964. PMID ...
FA, N-(4-{[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-glutamic acid, pteroyl-L-glutamic acid, vitamin B9,[ ... Folic acid is essential for the body to make DNA, RNA, and metabolise amino acids, which are required for cell division. Not ... 2S)-2-[[4-[(2-Amino-4-oxo-1H-pteridin-6-yl)methylamino]benzoyl]amino]pentanedioic acid[5] ... Folinic acid is not the same as folic acid. Folic acid supplements have little established role in cancer chemotherapy.[46][47] ...
Amino acid metabolism[edit]. *PLP is a cofactor in the biosynthesis of five important neurotransmitters: serotonin, dopamine, ... Its active form, pyridoxal 5′-phosphate, serves as a coenzyme in some 100 enzyme reactions in amino acid, glucose, and lipid ... Transaminases break down amino acids with PLP as a cofactor. The proper activity of these enzymes is crucial for the process of ... An estimated 40-60% of ingested vitamin B6 is oxidized to 4-pyridoxic acid. Several studies have shown that 4-pyridoxic acid is ...
"Analysis of the genomic organization of the human cationic amino acid transporters CAT-1, CAT-2 and CAT-4". Amino Acids. 21 (2 ... Cationic amino acid transporter 2 is a protein that in humans is encoded by the SLC7A2 gene.[5][6] ... cellular amino acid metabolic process. • nitric oxide production involved in inflammatory response. • L-arginine transport. • ... amino acid transport. • regulation of macrophage activation. • transmembrane transport. • L-lysine transmembrane transport. ...
FA, N-(4-{[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-glutamic acid, pteroyl-L-glutamic acid, vitamin B9,[ ... 2S)-2-[[4-[(2-Amino-4-oxo-1H-pteridin-6-yl)methylamino]benzoyl]amino]pentanedioic acid[5] ... Folic acid is essential for the body to make DNA, RNA, and metabolise amino acids, which are required for cell division.[10] As ... "Folic_Acid_msds".. *^ a b c d e f g h i "Folate". Micronutrient Information Center, Linus Pauling Institute, Oregon State ...
... s can bind to a messenger RNA chain and use its sequence for determining the correct sequence of amino acids. Amino ... It is during this binding that the correct translation of nucleic acid sequence to amino acid sequence occurs. For each coding ... As amino acids gradually appeared in the RNA world under prebiotic conditions,[54][55] their interactions with catalytic RNA ... The attached amino acids are then linked together by another part of the ribosome. Once the protein is produced, it can then ...
Amino acid[edit]. Cortisol raises the free amino acids in the serum by inhibiting collagen formation, decreasing amino acid ... Omega-6, omega-3 essential fatty acid ratio: the scientific evidence. Basel: Karger. p. 50. ISBN 978-3-8055-7640-6.. ... Omega-3 fatty acids have a dose-dependent effect[70] in slightly reducing cortisol release influenced by mental stress,[71] ... Cortisol stimulates gastric-acid secretion.[31] Cortisol's only direct effect on the hydrogen-ion excretion of the kidneys is ...
Proteins and amino acids[edit]. Alpha-carbon (α-carbon) is also a term that applies to proteins and amino acids. It is the ... The α-carbon of an amino acid is significant in protein folding. When describing a protein, which is a chain of amino acids, ... one often approximates the location of each amino acid as the location of its α-carbon. In general, α-carbons of adjacent amino ... That is, the groups hanging off the chain at the α-carbon are what give amino acids their diversity. These groups give the α- ...
Amino acid biosynthesis[edit]. All amino acids are formed from intermediates in the catabolic processes of glycolysis, the ... Amino acid biosynthesis from intermediates of glycolysis and the citric acid cycle. ... Pyruvate can come from the breakdown of glucose, lactate, amino acids, or glycerol.[10] The gluconeogenesis pathway has many ... From the citric acid cycle, α-ketoglutarate is converted into glutamate and subsequently glutamine, proline, and arginine; and ...
Amino acid synthesis. Chloroplasts alone make almost all of a plant cell's amino acids in their stroma[158] except the sulfur- ... Chloroplasts carry out a number of other functions, including fatty acid synthesis, much amino acid synthesis, and the immune ... Chloroplasts synthesize all the fatty acids in a plant cell[145][147]-linoleic acid, a fatty acid, is a precursor to jasmonate. ... This polypeptide has four amino acids linked together. At the left is the N-terminus, with its amino (H2N) group in green. The ...
Amino acid propensities[edit]. Large aromatic residues (tyrosine, phenylalanine, tryptophan) and β-branched amino acids ( ... A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The ... The side chains from the amino acid residues found in a β-sheet structure may also be arranged such that many of the adjacent ... However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, ...
... s range in size from 12 to 80 amino acid residues and have a wide range of structures.[8] Most cathelicidins are ... Even larger cathelicidin peptides (39-80 amino acid residues) are also present. These larger cathelicidins display repetitive ... although amino acid residues thought to be important in such protease inhibition are usually lacking. ... linear peptides with 23-37 amino acid residues, and fold into amphipathic α-helices. Additionally cathelicidins may also be ...
... beyond the twenty canonical amino acids found in nature, to include an unnatural amino acid as well. The unnatural amino acid ... the tRNA with the amino acid. Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing ... and redox-active amino acids.[14] Another use is introducing amino acids bearing reactive functional groups for chemically ... the cavity that holds the amino acid can be mutated and modified to carry unnatural amino acids synthesized in the lab, and to ...
... derived from the related proteinogenic L-amino acid glutamic acid. Theanine is an analog of this amino acid, and its primary ... is an amino acid analogue of the proteinogenic amino acids L-glutamate and L-glutamine and is found primarily in particular ... Not to be confused with threonine, a distinct amino acid, or theine, an archaic synonym of caffeine. ... Amino acids as oral immunomodulative nutrients". SpringerPlus. 2: 635. doi:10.1186/2193-1801-2-635. PMC 3851524. PMID 24312747. ...
Amino Acids. 40 (5): 1369-1383. doi:10.1007/s00726-011-0874-6. PMC 3080578 . PMID 21424716. UNeMed 2003 Annual Report, p.4 " ... Creatine gluconate is a form of creatine where the molecule is bound to gluconic acid. In 1912, Harvard University researchers ... annual meeting demonstrated that the addition of the ethyl group to creatine actually reduces acid stability and accelerates ...
Hornykiewicz O (2002). "L-DOPA: from a biologically inactive amino acid to a successful therapeutic agent". Amino Acids. 23 (1- ... The results regarding fat and fatty acids have been contradictory, with various studies reporting protective effects, risk- ...
ANSWER: amino acids. [10] During translation, amino acids are polymerized by these complexes, which are formed in the nucleolus ... A bonus question on amino acids. These biological monomers are usually in a zwitterionic form. For 10 points each:. [10] Name ...
The α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (also known as AMPA receptor, AMPAR, or quisqualate receptor ... A 38-amino acid sequence found prior to (i.e., before the N-terminus of) the fourth membranous domain in all four AMPAR ... While the amino acid sequence of the subunit indicated that there seemed to be four transmembrane domains (parts of the protein ... Here, A→I editing alters the uncharged amino acid glutamine (Q) to the positively charged arginine (R) in the receptor's ion ...
"Hydrophobic amino acids". Amino Acid Properties and Consequences of Substitutions, In: Bioinformatics for Geneticists. Wiley. ... and glutamic acid. While glutamic acid is usually sufficient because amino acid nitrogen is recycled through glutamate as an ... Cysteine (symbol Cys or C;[3] /ˈsɪstiiːn/)[4] is a semiessential[5] proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH ... interactions in micelles to a greater degree than the side chain in the nonpolar amino acid glycine and the polar amino acid ...
HMB is a metabolite of the amino acid leucine (Van Koverin and Nissen 1992), an essential amino acid. The first step in HMB ... Isovaleryl-coenzyme A, also known as isovaleryl-CoA, is an intermediate in the metabolism of branched-chain amino acids.[1][2][ ... fatty acids, and other compounds. Figure 8.57: Metabolism of L-leucine ...
"Hydrophobic amino acids". Amino Acid Properties and Consequences of Substitutions, In: Bioinformatics for Geneticists. Wiley. ... so it must be biosynthesized from its constituent amino acids, cysteine, glycine and glutamic acid. Glutamic acid and glycine ... Cysteine (symbol Cys or C;[3] /ˈsɪstiiːn/)[4] is a semi-essential[5] proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH ... interactions in micelles to a greater degree than the side chain in the non-polar amino acid glycine and the polar amino acid ...
AA: amino acids. • HMB: β-hydroxy β-methylbutyric acid. • ↑ represents activation. • Τ represents inhibition ... Many amino acids derived from food protein promote the activation of mTORC1 and increase protein synthesis by signaling through ... PA: phosphatidic acid. • mTOR: mechanistic target of rapamycin. • AMP: adenosine monophosphate. • ATP: adenosine triphosphate. ... in myofibrillar muscle protein synthesis and mitochondrial biogenesis in response to physical exercise and specific amino acids ...
The ultimate form of mature cathepsin D is composed of 337 amino acid residues, 196 amino acid residues in the heavy chain and ... The catalytic sites of cathepsin D include two critical aspartic residues (amino acid 33 and 231) located on the 14 kDa and ... cathepsin D accommodates up to 8 amino acid residues in the binding cleft of the active site. The main physiological functions ... "Nucleic Acids Research. 15 (9): 3773-86. doi:10.1093/nar/15.9.3773. PMC 340781 . PMID 3588310.. ...
... is an amino acid that has a single hydrogen atom as its side chain. It is the simplest amino acid (since carbamic acid is ... With acid chlorides, one obtains the amidocarboxylic acid, such as hippuric acid[23] and acetylglycine.[24] With nitrous acid, ... Amino acid neurotransmitter. References[edit]. *^ The Merck Index: An Encyclopedia of Chemicals, Drugs, and Biologicals (11th ... "Organic Molecule, Amino Acid-Like, Found In Constellation Sagittarius 27 March 2008 - Science Daily". Retrieved 2008-09-16.. ...
HMB is a metabolite of the amino acid leucine (Van Koverin and Nissen 1992), an essential amino acid. The first step in HMB ... fatty acids, and other compounds. Figure 8.57: Metabolism of L-leucine ...
PelB (an amino acid signal sequence that targets the protein to the periplasm where a signal peptidase then cleaves off PelB) ... Usually peptides that can be fused to pVIII are 6-8 amino acids long. The size restriction seems to have less to do with ... Moreover, pIII allows for the insertion of larger protein sequences (>100 amino acids) and is more tolerant to it than pVIII. ... Direct Interaction Rescue or by adding an 8-10 amino acid linker between the cDNA and pIII at the C-terminus. pVIII is the main ...
... they are simply converted into other amino acids. However, like other amino acids, BCAAs may interfere with medications for ... Branched-chain amino acid supplementation during repeated prolonged skiing exercises at altitude. Int J Sport Nutr. 1996;6:295- ... Amino acid supplements to improve athletic performance. Curr Opin Clin Nutr Metab Care. 1999;2:539-544. ... Branched-chain amino acids enhance the cognitive recovery of patients with severe traumatic brain injury. Arch Phys Med Rehabil ...
Heavy Subunits of the Heteromeric Amino Acid Transporter Family research products from R&D Systems. Learn more. ... Heavy Subunits of the Heteromeric Amino Acid Transporter Family research area related information and SLC3: ... Home » Research Areas » SLC3: Heavy Subunits of the Heteromeric Amino Acid Transporter Family ...
Branched-chain amino acids come together and discuss about Branched-chain amino acids. Please use the message board below to ... Amino acids Forum. • Aliphatic Forum. • Leucine Forum. • Isoleucine Forum. • Valine Forum. • Branched chain aminotransferase ... There are no entries in Branched-chain amino acids forum. Become the first person to post messages in this forum by using the ... Congratulations! You have found the Branched-chain amino acids Forum on Forum Jar. This forum is a place where people who are ...
ranched-chain amino acids (BCAAs: leucine, isoleucine and valine) are essential amino acids for humans and animals. It has been ... Branched-chain amino acids (BCAAs) as nutraceuticals for exercise. Branched-chain amino acids (BCAAs) as nutraceuticals for ... shown that BCAA oxidation is promoted by exercise through activation of branched-chain α-keto acid dehydrogenase complex (BCKDC ...
Unlike nonessential amino acids, essential amino acids cant be made by your body and must be obtained through your diet. ... What Are Essential Amino Acids?. Amino acids are organic compounds composed of nitrogen, carbon, hydrogen and oxygen, along ... Conditionally Essential Amino Acids. There are several nonessential amino acids that are classified as conditionally essential. ... The nine essential amino acids perform a number of important and varied jobs in your body:. *Phenylalanine: Phenylalanine is a ...
Two enzymes convert L-amino acids to D-amino acids. D-Amino-acid racemase, a PLP-dependent enzyme, racemizes amino acids via ... D-Amino acids are amino acids where the stereogenic carbon alpha to the amino group has the D-configuration. For most naturally ... L-amino-acid oxidases convert L-amino acids to the alpha-ketoacids, which are susceptible to reductive amination. Some amino ... L- and D-amino acids are usually enantiomers. The exceptions are two amino acids with two stereogenic centers, threonine and ...
Amino acids that must be obtained from the diet are called essential amino acids. Nonessential amino acids are produced in the ... Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The ... Commercial syntheses of amino acids[edit]. The commercial production of amino acids usually relies on mutant bacteria that ... Most amino acids are synthesized from α-ketoacids, and later transaminated from another amino acid, usually glutamate. The ...
Amino acids are the building blocks for proteins in the body. ... test done on infants that looks at the amounts of amino acids ... Plasma amino acids is a screening test done on infants that looks at the amounts of amino acids in the blood. Amino acids are ... Amino acids, peptides, and proteins. In: Rifai N, ed. Tietz Textbook of Clinical Chemistry and Molecular Diagnostics. 6th ed. ... An increased level of a particular amino acid is a strong sign. This shows that there is a problem with the bodys ability to ...
Strings of amino acids make up proteins, of which there are countless varieties. ... AMINO ACIDS CONCEPT Amino acids are organic compounds made of carbon, hydrogen, oxygen, nitrogen, and (in some cases) sulfur ... Only L-amino acids occur in proteins made by living systems. D-amino acids and amino acids other than α-amino acids occur in ... Amino Acid Biology COPYRIGHT 2002 The Gale Group Inc.. Amino Acid. Amino acids are molecules that have both an amino group (-NH ...
Amino acids are very important in our daily life as energy sources and have several functions in metabolism since amino acids ... All the amino acids contain a chiral carbon atom and they exist in d- and l-forms except one amino acids, i.e., glycine. ... Bhushan R, Bruckner H (2004) Marfeys reagent for chiral amino acid analysis: a review. Amino Acids 27:231-247PubMedCrossRef ... Bruckner H, Westhauser T (2003) Chromatographic determination of l- and d-amino acids in plants. Amino Acids 24:43-55PubMed ...
... the monoamide of glutamic acid, and an abundant constituent of proteins. First isolated from gliadin, a protein present in ... that is unique to each amino acid. The term amino acid. is short for α-amino [alpha-amino] carboxylic acid. . Each molecule… ... amino acid. Amino acid. , any of a group of organic molecules that consist of a basic amino group (―NH2), an acidic carboxyl ... Glutamine, an amino acid, the monoamide of glutamic acid, and an abundant constituent of proteins. First isolated from gliadin ...
When the carboxyl carbon atom of one amino acid covalently binds to the amino nitrogen atom of another amino acid with the ... The 20 amino acids commonly found in animals are alanine , arginine , asparagine , aspartic acid , cysteine , glutamic acid , ... Cellular catabolism breaks amino acids down into smaller fragments. Many of the amino acids necessary in metabolism can be ... and more than 100 less common amino acids also occur in biological systems, particularly in plants. Every amino acid except ...
8-tetracyanoquinodimethane were obtained by the condensation of the acid dichlorides of furan-2,5-dicarboxylic acid and... ... The corresponding amino esters and their complexes with 7,7,8, ... The corresponding amino esters and their complexes with 7,7,8,8 ... 5-dicarboxylic acid and tetrahydrothiophene-2,5-dicarboxylic acid with 8-hydroxy- and 5,7-dibromo-8-hydroxyquinolines. Almost ... Ester Organic Chemistry Antimicrobial Activity Dicarboxylic Acid Dichloride Translated from Khimiya Geterotsiklicheskikh ...
Disclosed are β-amino acid monomers containing cylcoalkyl, cycloalkenyl, and heterocylic substituents which encompass the α and ... For unsubstituted β-amino acids and β-amino acids containing one or two acyclic substituents on the carbon adjacent to the ... Podlech and Seebach (1995) On the Preparation of β-Amino Acids from α-Amino Acids Using the Arndt-Eistert Reaction: Scope, ... The amino group of each subsequent amino acid to be added to the N-terminus of the growing peptide chain is protected with Boc ...
D-amino acid (CHEBI:21501) is a N-acetyl-amino acid (CHEBI:21575). N-acetyl-L-amino acid (CHEBI:21545) is a N-acetyl-amino acid ... acetic acid (CHEBI:15366) N-acetyl-amino acid (CHEBI:21575) is a N-acyl-amino acid (CHEBI:51569) N-acetyl-amino acid (CHEBI: ... N2-acetylglutamine (CHEBI:73685) is a N-acetyl-amino acid (CHEBI:21575). grixazone A (CHEBI:73546) is a N-acetyl-amino acid ( ... N-acetylcitrulline (CHEBI:49006) is a N-acetyl-amino acid (CHEBI:21575). N-acetylglycine (CHEBI:40410) is a N-acetyl-amino acid ...
L-α-amino acid (CHEBI:15705) is a α-amino acid (CHEBI:33704) L-α-amino acid (CHEBI:15705) is conjugate acid of L-α-amino acid ... L-α-amino acid (CHEBI:15705). serine family amino acid (CHEBI:26650) is a L-α-amino acid (CHEBI:15705). L-α-amino acid anion ( ... glutamine family amino acid (CHEBI:24318) is a L-α-amino acid (CHEBI:15705). LSM-11903 (CHEBI:100529) is a L-α-amino acid ( ... L-α-amino acid residue (CHEBI:83228) is substituent group from L-α-amino acid (CHEBI:15705). L-α-amino acid zwitterion (CHEBI: ...
D-amino acids be structural mirror images of L-amino acids.) All amino acids have the same "backbone", or basic structure:. ... This will create an amino nitrile. To this add aqueous acid, heat, and water, and voila, an amino acid.. Organic Chemistry: ... An amino acid is a carbon atom with a hydrogen atom, an organic acid {COOH}, an amino group {NH2}, and one other chemical group ... Amino acids are the building blocks of proteins. The following is one of several ways to synthesize amino acids. Its advantage ...
A ball-and-stick model structure of polar amino acid glutamine (Gln, Q). Carbon in blue-grey, oxygen in red, nitrogen in green ... Glutamine (amino acid). By. J_Alves. Created. 2010-05-20. Description. A ball-and-stick model structure of polar amino acid ... acid , amino , amino acid , biology , chemistry , glutamine , model , polar , science , structure. Viewed by. 3342 People. ...
... Mark Lamkin mlamkin at acs.bu.edu Mon Jan 23 16:51:24 EST 1995 *Previous message: Help! Blocked ... I am looking for a method to separate pth-amino acids using a C18 column. Wonder if any out there can help in my application. ...
Can you pick the correct structure for each amino acid? Test your knowledge on this science quiz to see how you do and compare ... Tags:Biology Quiz, Chemistry Quiz, amino, Amino Acids, formula, Organic Chemistry, Picture Click, protein, skeletal, structure ... Science Quiz / Amino Acids by Structure. Random Science or Organic Chemistry Quiz ... Can you pick the correct structure for each amino acid?. by Scuadrado ...
Olefi n moieties open amino acids and peptides to metathesis reactions and a full range of other bioorthogonal synthesis routes ... Recent developments in Chemical Biology research have increased the demand of amino acid building blocks with unsaturated side ...
Influence of a number of amino acids on the rate of reaction has been studied at several additive concentrations. The addition ... On the basis of the obtained results, it is possible to develop technologically accessible electrodialysis of amino acids as ... Keywords: Amino acids; Chiral recognition; Electrodialysis; Membrane; Molecular imprinting; Molecular recognition; Optical ... Desalting of neutral amino acids fermentative solutions by electrodialysis with ion-exchange membranes ...
Unnatural Amino Acids II, ß-Amino Acids and Homo Amino Acids . ChemFiles Vol 2 No 4 . ... Cyclic Amino Acids / Diamino Acids / ß-Amino Acids and Homo Amino Acids. Alanine Derivatives / Phenylalanine Boronic Acids / ... ß-Amino Acids and Homo Amino Acids. In the past few years ß-peptides and other ß-amino acid containing oligomers have emerged ... ß-amino acid by an ß-amino acid residue resulted in a hybrid oligopeptide which binds to major histocompatibility complex (MHC ...
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The α-carbon atom of all amino acids, with the exception of glycine, is asymmetric; this means that four different chemical ... As a result, each of the amino acids, except glycine, can exist in two different spatial, or geometric, arrangements (i.e., ... The physicochemical properties of a protein are determined by the analogous properties of the amino acids in it. ... Amino acid sequence in protein molecules. Since each protein molecule consists of a long chain of amino acid residues, linked ...
  • It has been shown that BCAA oxidation is promoted by exercise through activation of branched-chain α-keto acid dehydrogenase complex (BCKDC), which is a rate-limiting enzyme in the catabolic pathway of the BCAAs, and the elevated enzyme activity in skeletal muscle is quickly downregulated after exercise. (e-pan.org)
  • All the amino acids contain a chiral carbon atom and they exist in d- and l -forms except one amino acids, i.e., glycine. (springer.com)
  • As a result, each of the amino acids, except glycine, can exist in two different spatial, or geometric, arrangements (i.e., isomers ), which are mirror images akin to right and left hands. (britannica.com)
  • In fact, glycine is frequently used as a buffer in the pH range from 1 to 3 (acid solutions) and from 9 to 12 (basic solutions). (britannica.com)
  • In acid solutions, glycine has a positive charge and therefore migrates to the cathode (negative electrode of a direct-current electrical circuit with terminals in the solution). (britannica.com)
  • Most of the monoamino acids (i.e., those with only one amino group) have isoelectric points similar to that of glycine. (britannica.com)
  • If you look yet again at the general formula for an amino acid, you will see that (apart from glycine, 2-aminoethanoic acid) the carbon at the centre of the structure has four different groups attached. (chemguide.co.uk)
  • Because of these four different groups attached to the same carbon atom, amino acids (apart from glycine) are chiral . (chemguide.co.uk)
  • These are all L-stereoisomers ("left-handed" isomers), although a few D-amino acids ("right-handed") occur in bacterial envelopes, as a neuromodulator (D-serine), and in some antibiotics. (wikipedia.org)
  • We initially targeted for study 2-amino-2,3-dimethylpentanoic acid (2-a-2,3-dmpa), an amino acid with two chiral centers and, consequently, four stereoisomers ( 8 ) (Fig. 1 ). (sciencemag.org)
  • This amino acid meets two important criteria: (i) It is present in the Murchison meteorite ( 9 ) but has not been reported to occur in terrestrial matter, and (ii) its two chiral centers are resistant to epimerization because one (C-2) lacks a hydrogen atom and the other (C-3) has a methine hydrogen atom of low acidity. (sciencemag.org)
  • This amino acid has two chiral centers and, consequently, four stereoisomers: the D and L forms of α-methylisoleucine and α-methylalloisoleucine. (sciencemag.org)
  • Recently, GC was applied for chiral amino acid analysis on spacecrafts [ 11 ], such as the robotic lander Philae [ 12 ]. (hindawi.com)
  • The amino group can be taken from ammonia (NH 3 ) in the environment and used to make glutamate or glutamine. (dummies.com)
  • Here's the second frugal thing that microbes do: After glutamine and glutamate are made, the amino group can be used in all the other 20 amino acids. (dummies.com)
  • They are also known (slightly confusingly) as alpha-amino acids . (chemguide.co.uk)
  • In the alpha amino acids, the amino and carboxylate groups are attached to the same carbon atom, which is called the α-carbon. (medicalxpress.com)
  • The various alpha amino acids differ in which side chain (R group) is attached to their alpha carbon. (medicalxpress.com)
  • Over 30 unnatural amino acids have been inserted translationally into protein in engineered systems, yet are not biosynthetic. (wikipedia.org)
  • Further remarkable applications of ß-amino acids are the use as protease inhibitors, 11 precursors for antibiotics 12 and building blocks in cryptophycins. (sigmaaldrich.com)
  • Consequently, amino acids are also precursors of glucose , fatty acids, and ketone bodies and are therefore metabolic fuels. (conservapedia.com)
  • Amino acids ( Figure 1 ) play multiple important roles in our body: they are basic structural protein units and precursors of neurotransmitters, porphyrins, and nitric oxide. (intechopen.com)
  • Two enzymes convert L-amino acids to D-amino acids. (wikipedia.org)
  • Imipramine functionalized compounds are provided for conjugation to antigenic compounds, particularly poly(amino acids), and enzymes. (google.com)
  • Eating implies the material is being exposed to digestive enzymes and such, and since enzymes are very shape specific, the protein material being ingested probably wouldn't be broken down into component amino acids. (thenakedscientists.com)
  • Although over 100 amino acids exist in nature, the human body requires 20 amino acids, called standard amino acids , for normal functioning. (newworldencyclopedia.org)
  • Chemical structures of the 20 standard amino acids. (newworldencyclopedia.org)
  • The standard amino acids thus exhibit the pattern 1 + 19. (newworldencyclopedia.org)
  • These non-standard amino acids do not have a dedicated codon, but are added in place of a stop codon when a specific sequence is present, UGA codon and SECIS element for selenocysteine, UAG PYLIS downstream sequence for pyrrolysine. (wikipedia.org)
  • Of the basic set of twenty amino acids (not counting selenocysteine ), humans cannot synthesize eight. (wikipedia.org)
  • Animals can synthesize certain amino acids. (newworldencyclopedia.org)
  • Although all vertebrates require certain amino acids that their cells cannot synthesize, ruminant animals (such as cattle ) carry within one of the stomachs microbes that synthesize the amino acids needed by the animals. (newworldencyclopedia.org)
  • Living organisms constantly break down certain amino acids and compounds, then synthesize them to create the amino acids that organism needs. (wisegeek.com)
  • Nucleotides are the subunits of nucleic acids like ribonucleic acid (RNA) and deoxyribonucleic acid (DNA), and like amino acids they're expensive and time consuming to make. (dummies.com)
  • With the exception of α-amino- n -butyric acid, these amino acids are either unknown or of limited occurrence in the biosphere. (sciencemag.org)
  • Clostridium botulinum type F (proteolytic), C. ghoni, C. mangenoti and C. putrificum were found to reduce proline to 5-aminovaleric acid and to produce 2-aminobutyric acid, properties they shared with C. sporogenes and C. sticklandii. (nih.gov)
  • Most amino acids are synthesized from α- ketoacids , and later transaminated from another amino acid, usually glutamate . (wikipedia.org)
  • At this step, the chirality of the amino acid is established. (wikipedia.org)
  • In addition, the chirality (structure) of the amino acids in the meteorite is closer to that of amino acids that are found in organisms on Earth, which are all left-handed, than the structure predicted for amino acids produced through chemical reactions in space, which are predicted to be equally left and right-handed. (encyclopedia.com)
  • Amino acids come in two types, left-handed and right-handed (called chirality). (thenakedscientists.com)
  • Some amino acids contain the opposite absolute chirality, chemicals that are not available from normal ribosomal translation/transcription machinery. (wikipedia.org)
  • Many D-amino acids found in higher organisms are derived from microbial sources. (wikipedia.org)
  • Once used in dating objects from the distant past, amino acids have existed on Earth for at least three billion years - long before the appearance of the first true organisms. (encyclopedia.com)
  • Accordingly, living organisms are classified as being either ammonotelic (ammonia excreting), ureotelic (urea excreting), or uricotelic (uric acid excreting). (conservapedia.com)
  • The polyamide layer technique for the chromatographic separation of dimethylaminonaphthalene sulphonyl amino acids has been adapted to the qualitative analysis of amino acids in media before and after the growth of micro-organisms. (nih.gov)
  • These include spoilage organisms such as Brettanomyces , Acetobacter and Lactic acid bacteria from the Lactobacillus and Pediococcus genera . (wn.com)
  • Certain organisms, such as plants and yeast, can produce all 20 amino acids on their own. (wisegeek.com)
  • D amino acids do crop up in L- amino dependent organisms, but usually in a pathological context. (thenakedscientists.com)
  • So, organisms (on earth) are composed of L-amino acids, but there are trace amounts of D-forms. (thenakedscientists.com)
  • Some non-α amino acids exist in organisms. (wikipedia.org)
  • Aside from those two special cases, L- and D-amino acids have identical properties (color, solubility, melting point) under many conditions. (wikipedia.org)
  • At this point I would normally try to relate the actual values for solubility of the various amino acids to their structures. (chemguide.co.uk)