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)

*Protein metabolism

... and production of glucose or fat or other amino acids. This break-down of amino acids to α-keto acids occurs in the liver by a ... anabolic amino acid synthesis). Protein catabolism is the process by which proteins are broken down to their amino acids. This ... These amino acids are further broken down to α-keto acids which can be recycled in the body for generation of energy, ... Dietary proteins are first broken down to individual amino acids by various enzymes and hydrochloric acid present in the gastro ...

*Essential amino acid

An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized de novo (from scratch) by the ... amino acids are sometimes considered a single pool of nutritionally equivalent amino acids as are the aromatic amino acid pair ... amino acids Low-protein diet Orthomolecular medicine Protein Digestibility Corrected Amino Acid Score Ketogenic amino acid ... Amino acid content of some vegetarian foods at veganhealth.org. Amino Acid Profiles of Some Common Feeds at Virginia Tech. ...

*Protein primary structure

Amino acids are polymerised via peptide bonds to form a long backbone, with the different amino acid side chains protruding ... Protein sequencing Nucleic acid primary structure Translation Pseudo amino acid composition SANGER F (1952). "The arrangement ... listing the amino acids starting at the amino-terminal end through to the carboxyl-terminal end. Either a three letter code or ... as well as mixtures or ambiguous amino acids (similar to nucleic acid notation). Peptides can be directly sequenced, or ...

*SLC1A1

Excitatory amino-acid transporter 3 is a member of the high-affinity glutamate transporters which plays an essential role in ... SLC1A1, also known as excitatory amino-acid transporter 3 (EAAT3), is a protein that in humans is encoded by the SLC1A1 gene. ... Excitatory amino acid transporter Glutamate transporter Solute carrier family GRCh38: Ensembl release 89: ENSG00000106688 - ... Nieoullon A, Canolle B, Masmejean F, Guillet B, Pisano P, Lortet S (2006). "The neuronal excitatory amino acid transporter ...

*Amino acid

Only 837 D-amino acids were found in Swiss-Prot database (187 million amino acids analysed). The 20 amino acids that are ... part of amino acid catabolism (see below). A rare exception to the dominance of α-amino acids in biology is the β-amino acid ... "N-alkylated alpha-amino acid". The α-carboxylic acid group of amino acids is a weak acid, meaning that it releases a hydron ( ... While L-amino acids represent all of the amino acids found in proteins during translation in the ribosome, D-amino acids are ...

*Non-proteinogenic amino acids

There are various groups of amino acids: 20 standard amino acids 22 proteinogenic amino acids over 80 amino acids created ... ic acid.) Most natural amino acids are α-amino acids in the L conformation, but some exceptions exist. Some non-α amino acids ... a β-amino acid. Taurine is an amino sulfonic acid and not an amino acid, however it is occasionally considered as such as the ... amino acids. Other amino acids are solely found in abiotic mixes (e.g. α-methylnorvaline). Over 30 unnatural amino acids have ...

*Amino acid kinase

The conversion of aspartate into either the storage amino acid asparagine or aspartate family amino acids may be subject to a ... In molecular biology, the amino acid kinase domain is a protein domain. It is found in protein kinases with various ... In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed- ... relatively little is known about the regulation of carbon and nitrogen flow into amino acids. The metabolic regulation of ...

*Proteinogenic amino acid

The abundance of amino acids includes amino acids in free form and in polymerization form (proteins). The proteinogenic set ... Glucogenic amino acid Ketogenic amino acid Ambrogelly A, Palioura S, Söll D (Jan 2007). "Natural expansion of the genetic code ... Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word " ... In contrast, non-proteinogenic amino acids are amino acids that are either not incorporated into proteins (like GABA, L-DOPA, ...

*Amino acid transporter

Solute carrier family Amino acid transport Amino acid transport, acidic Amino acid transport, basic Amino acid transport ... An amino acid transporter is a membrane transport protein that transports amino acids. They are mainly of the solute carrier ... There are several families that function in amino acid transport, some of these include: TC# 2.A.3 - Amino Acid-Polyamine- ... Branched Chain Amino Acid Exporter (LIV-E) Family TC# 2.A.95 - 6TMS Neutral Amino Acid Transporter (NAAT) Family TC# 2.A.118 - ...

*Aromatic amino acid

An aromatic amino acid (AAA) is an amino acid that includes an aromatic ring. Examples include: Among 20 standard amino acids: ... Aromatic amino acids are able to absorb light due to their conjugated double bonds. This characteristic of aromatic amino acids ... Animals obtain aromatic amino acids from their diet, but all plants and micro-organisms must synthesize their aromatic amino ... These amino acids are able to absorb light which excites its electron to the excited state. When the electron falls back to its ...

*Amino acid oxidoreductases

... are oxidoreductases, a type of enzyme, that act upon amino acids. They constitute the majority of ... Examples include: Glutamate dehydrogenase Nitric oxide synthase Amino Acid Oxidoreductases at the US National Library of ...

*Amino acid response

... (AAR) is the mechanism triggered in mammalian cells by amino acid starvation. The amino acid response ... is a cofactor of ATF4 for amino acid-regulated transcription of CHOP". Nucleic Acids Res. 35 (17): 5954-65. doi:10.1093/nar/ ... Amino acid deprivation induces the transcription rate of the human asparagine synthetase gene through a timed program of ... Kilberg MS, Pan YX, Chen H, Leung-Pineda V. Nutritional control of gene expression: how mammalian cells respond to amino acid ...

*Amino acid permease

... s are membrane permeases involved in the transport of amino acids into the cell. A number of such proteins ... Amino acid transporter CIP1; SLC12A1; SLC12A2; SLC12A3; SLC12A4; SLC12A5; SLC12A6; SLC12A7; SLC12A8; SLC12A9; SLC7A1; SLC7A10; ...

*Glucogenic amino acid

Ketogenic amino acid List of standard amino acids Glycolysis Metabolism Brosnan J (1 June 2003). "Interorgan amino acid ... The production of glucose from glucogenic amino acids involves these amino acids being converted to alpha keto acids and then ... A glucogenic amino acid is an amino acid that can be converted into glucose through gluconeogenesis. This is in contrast to the ... Amino acid metabolism Chapter on Amino acid catabolism in Biochemistry by Jeremy Berg, John Tymoczko, Lubert Stryer. Fourth ed ...

*Amino acid activation

... During amino acid activation the amino acids (aa) are attached to their corresponding tRNA. The coupling ... Amino acid activation refers to the attachment of an amino acid to its Transfer RNA (tRNA). Aminoacyl transferase binds ... to amino acid, PP is released. Aminoacyl transferase binds AMP-amino acid to tRNA. The AMP is used in this step. ... one specific amino acid and its corresponding tRNA. The specificity of the amino acid activation is as critical for the ...

*Amino acid score

... , in combination with protein digestibility, is the method used to determine if a protein is complete. PDCAAS ... two major protein standards which determine the completeness of proteins by their unique composition of essential amino acids. ...

*Amino acid neurotransmitter

There are inhibitory amino acids (IAA) or excitatory amino acids (EAA). Some EAA are L-Glutamate, L-Aspartate, L-Cysteine, and ... An amino acid neurotransmitter is an amino acid which is able to transmit a nerve message across a synapse. Neurotransmitters ( ... Amino acid non-protein functions Monoamine neurotransmitter "Axon Terminal : on Medical Dictionary Online". Archived from the ... Amino acid neurotransmitter release (exocytosis) is dependent upon calcium Ca2+ and is a presynaptic response. ...

*Amino acid synthesis

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 various amino acids are produced ... Most amino acids are synthesized from α-ketoacids, and later transaminated from another amino acid, usually glutamate. The ... A transamination reaction takes place in the synthesis of most amino acids. At this step, the chirality of the amino acid is ...

*Amino acid replacement

... is a change from one amino acid to a different amino acid due to point mutation in DNA sequence. It is ... Leucine is an example of a typical amino acid. Idiosyncratic amino acids - there are few similar amino acids that they can ... or simple properties such as amino acid size or charge (see also amino acid chemical properties). Usually amino acids are thus ... Amino acids can also be classified according to how many different amino acids they can be exchanged by through single ...

*Ketogenic amino acid

Glucogenic amino acid List of standard amino acids Ketogenesis Metabolism Amino acid metabolism Chapter on Amino acid ... two amino acids are exclusively ketogenic: (remembered as all the "L" amino acids) Leucine Lysine In humans, five amino acids ... A ketogenic amino acid is an amino acid that can be degraded directly into acetyl-CoA, which is the precursor of ketone bodies ... This is in contrast to the glucogenic amino acids, which are converted into glucose. Ketogenic amino acids are unable to be ...

*Amino acid dating

Amino acid racemization analysis consists of sample preparation, isolation of the amino acid wanted, and measure of its D:L ... All biological tissues contain amino acids. All amino acids except glycine (the simplest one) are optically active, having a ... Fundamentals of sample age determination from its amino acid racemization by Policarp Hortolà Brown 1985 Amino Acid Dating. ... Origins 12(1):8-25 Northern Arizona University Amino Acid Geochronology Laboratory University of Massachusetts Amino Acid ...

*Amino-acid racemase

... a D-amino acid Hence, this enzyme has one substrate, L-amino acid, and one product, D-amino acid. This enzyme belongs to the ... In enzymology, an amino-acid racemase (EC 5.1.1.10) is an enzyme that catalyzes the chemical reaction an L-amino acid ⇌ {\ ... The systematic name of this enzyme class is amino-acid racemase. This enzyme is also called L-amino acid racemase. This enzyme ... Soda K, Osumi T (1969). "Crystalline amino acid racemase with low substrate specificity". Biochem. Biophys. Res. Commun. 35 (3 ...

*ADDA (amino acid)

6-dienoic acid is a non-proteinogenic amino acid found in toxins made by cyanobacteria. Toxins which include this amino acid ... all-S,all-E)-3-Amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4, ...

*D-amino acid oxidase

DAO DAOA-AS1 D-amino acid dehydrogenase D-amino acid oxidase activator D-aspartate oxidase Diamine oxidase D-Amino-Acid Oxidase ... The enzyme is most active toward neutral D-amino acids, and not active toward acidic D-amino acids. DAAO is a candidate ... It is not present in plants or in bacteria which instead use D-amino acid dehydrogenase. Its function is to oxidize D-amino ... this is then hydrolysed to yield ammonia and the corresponding a-keto acid." Recently, mammalian D-amino acid oxidase has been ...

*Amino acid N-carboxyanhydride

... s, also called Leuchs' anhydrides, are reactive derivatives of amino acids. They are classified as ... NCA's are precursors to amino acid homopolymers. Ephraim Katzir first used this method to synthesize poly-L-lysine from N- ... NCA's were first synthesized in 1906 by Hermann Leuchs by heating an N-ethoxycarbonyl or N-methoxycarbonyl amino acid chloride ... Typically these compounds are derived from amino acids by treatment with triphosgene. They are white solids, prone to ...

*Phage display

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 ...

*Heterodimeric amino-acid transporter

... s are a family of transport proteins that facilitate the transport of certain amino acids ... "Function and structure of heterodimeric amino acid transporters". Am. J. Physiol., Cell Physiol. 281 (4): C1077-93. PMID ...
Before Its News). The Non-Essential Amino Acids Market Research Report is a comprehensive analysis of the market with a chapter wise explanation of each important aspect. The thorough analysis in this report enables one to understand the market in a better way and based on that knowledge make well-informed decisions.. Detailed TOC and Charts & Tables of Non-Essential Amino Acids Market Research Report available at- http://www.absolutereports.com/global-non-essential-amino-acids-market-research-report-2016-n-10357909. Product Types of Non-Essential Amino Acids:. • Arginine. • Asparagine. • Aspartic Acid. • L-Cysteine. • Glutamic Acid. • Glutamine. The Non-Essential Amino Acids market overview is given in the first three chapters of this report. Definitions and classifications of the market are explained in this part and industry chain structure is explained. Various policies and news are also included. Various costs involved in the production of Non-Essential Amino Acids are ...
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 ...
N-Acetyl Cysteine is powerful antioxidant, anti-toxin, and immune support compound which is the simpler and more bioavailable form of the non-essential amino acid Cysteine, this derivative is also being a precursor to Glutathione.
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
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 ...
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
Noncanonical amino acids (NCAAs) can be used in a variety of protein design contexts. For example, they can be used in place of the canonical amino acids (CAAs) to improve the biophysical properties of peptides that target protein interfaces. We describe the incorporation of 114 NCAAs into the protein-modeling suite Rosetta. We describe our methods for building backbone dependent rotamer libraries and the parameterization and construction of a scoring function that can be used to score NCAA containing peptides and proteins. We validate these additions to Rosetta and our NCAA-rotamer libraries by showing that we can improve the binding of a calpastatin derived peptides to calpain-1 by substituting NCAAs for native amino acids using Rosetta. Rosetta (executables and source), auxiliary scripts and code, and documentation can be found at (http://www.rosettacommons.org/).
... s, also known as standard, normal, or primary amino acids, are those 20 amino acids that are found in proteins
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 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.
Glycine, the Wound Healer. Glycine is an amino acid that tastes sweet like sugar, and it is the only amino acid the liver can use in place of glucose. High insulin levels suck glucose out of the bloodstream into the liver for storage as glycogen.
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 ...
Protein is made up of 20 amino acids. Every type of protein is made of a different combination of amino acids and all of them are necessary to human life. Of those 20 amino acids, half are known as non-essential amino acids and the other half are called essential amino acids. Non-essential amino acids are […]. ...
Tyrosine.. Another method uses the first letter of each essential amino acid to begin each word in a phrase, such as: "Any Help in Learning These Little Molecules Proves Truly Valuable. It solution begins with the two amino acids that need some qualifications as to their requirements. This is not necessity to consume plant foods containing comprehensive proteins as long as a fairly different diet is maintained.. ...
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.. ...
Arginine is classified as a non-essential amino acid since our bodies can produce it. But, because it becomes limiting in many circumstances, its usually referred to as conditionally dispensable. Arginine is the rate limiting amino acid in the synthesis of NO. Increasing the bioavailability of NO improves dilation of blood vessels and reduces blood pressure. Emerging evidence suggests exercise efficiency and performance may benefit as well.For nitric oxide and growth hormoneArginine is classified as a non-essential amino acid since our bodies can produce it. But, because it becomes limiting in many circumstances, its usually referred to as conditionally dispensable.. Arginine is the rate limiting amino acid in the synthesis of NO. Increasing the bioavailability of NO improves dilation of blood vessels and reduces blood pressure. Emerging evidence suggests exercise efficiency and performance may benefit as well. In one study, healthy men who consumed 6g of arginine reduced the amount of oxygen ...
Branched-chain amino acid supplements have been shown to help decrease muscle soreness and damage and increase protein synthesis in your body after...
There are 22 amino acids used by the human body. Of these, some are considered essential amino acids (including isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine), meaning the body cannot create them. These must be supplied by an external source such as a food or supplement.. The remaining compounds are nonessential amino acids (including alanine, arginine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine and tyrosine), which the body can generate. However, this does not necessarily guarantee that enough of these amino acids are produced. Additional amounts from diet and/or supplementation are often needed.. Common dietary sources of amino acids are dairy and meat products and eggs, which contain all essential amino acids. Other foods rich in some, but not all, amino acids include beans, legumes, nuts, apples and pears.. Branched chain amino acid (BCAA) supplements have become popular with bodybuilders and athletes. Supplying ...
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.. ...
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View Notes - Lecture 13 amino acid synthesis from BIOLCHEM 415 at University of Michigan. BergTymoczkoStryer Biochemistry Chapter24: TheBiosynthesisofAminoAcids CopyrightbyW.H.FreemanandCompany Overvi
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Dietary Supplement. Anabolic Liquid. Mass. The Science Behind the Size: Product-A fast absorbing anabolic liquid amino acid that has, per serving, 15 grams (15,000 mg) of high quality branched chain, peptide-bonded, and free amino acids; Stress B-Complex Vitamins; Energizing complex carbohydrates; and pure crystalline fructose. Result-Protein in its most easily digested, absorbable and utilizable form to maximize muscle growth and optimize protein synthesis. Science-Research shows that when taken orally, peptide-bonded amino acids increase nitrogen retention better than free form amino acid mixtures for optimum muscle growth. Essential Amino Acids: L-Leucine (BCAA), L-Isoleucine (BCAA), L-Valine (BCAA), L-Lysine, L-Threonine, L-Methionine, L-Phenylalanine, L-Tryptophan. Non-Essential Amino Acids: L-Arginine, L-Cystine, L-Alanine, L-Aspartic Acid, L-Glutamic, L-Glycine, L-Histidine, L-Proline, L-Serine, L-Tyrosine. Essential Amino Acid; Branched Chain Amino Acids; The L-Tryptophan in this product ...
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Amino Acids supplements -These compounds are the building blocks of protein - the basis of life. What are the benefits of including them in your self-care program?
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In contrast to the specific signs that may occur as a result of vitamin or mineral deficiencies, the effects of essential amino acid deficiencies are nonspecific: reduced growth, reduced feed consumption, decreased egg production and egg size, and loss of body weight in adult hens. The decreased of feed intake occurs within hours of consumption of a deficient diet and is due to a distortion in plasma and tissue amino acid levels.. Practical ingredients usually are limiting in one or more amino acids. It is often cost effective to supply the limiting amino acids in the form of synthetic amino acids, especially lysine and methionine. Other amino acids such as threonine, tryptophan, arginine, and isoleucine can become limiting when unusual protein sources are used or when the dietary protein level is reduce. Diets that are devoid of animal by-products are often fortified heavily with feed-grade amino acids.. Marginal amino acid deficiencies often result in increased food intake, or the maintenance ...
Problem statement: Free Met as one of the most limiting AA in dairy cows would be mostly degraded in the rumen. This study was to determine the effect of different levels of Rumen-Protected Met (RPMet) on dairy performance and serum amino acid metabolism. Approach: Thirty-six Holstein cows in similar condition were randomly assigned to six experimental treatments with six replicates each. Levels of RPMet in six treatments were 0(control), 14, 28, 42, 56 and 70 g day-1 per cow, respectively. Results: Treatment had no effect on percentage of milk protein, lactose and SNF. However, milk yield of cows fed 42 g day-1 RPMet was significantly higher than that of the control group and milk fat percentage was significantly increased with 56 g day-1 RPMet supplementation. There was the trend to decrease the concentration of serum amino acids except Met and Arg with the supplementation of RPMet. Serum EAA contents of the group supplementation of 42 g day-1 RPMet were lowest although there were no significant
Low prices on Amino Acids! Amino acids are the most important nutrients for bodybuilders and strength trainers. Amino acids are used singly and in combination with other amino acids. Amino acids support protein synthesis and muscle building.*Branched chain amino acids (or BCAAs) have well-documented anti-catabolic benefits, helping to preserve muscle and lean body mass during intensive training and dieting periods.*
Fish do not have a specific protein requirement but rather a definite requirement for essential amino acids that comprise proteins. In other words, it is essential amino acids in dietary protein that a fish requires and not the protein per se. When protein is digested, the amino acids comprising it are released and absorbed into the body as either individual amino acids or shorter chains of amino acids, the di- and tri-peptides. There are about 20 known amino acids used as building blocks for the proteins in all living organisms. Ten amino acids are essential, and they must be incorporated into diets because fish either cannot synthesize them or can synthesize them at a rate that is inadequate for cellular demand. The other amino acids are classified as dispensable or dietary non-essentials because fish can synthesize them at a rate that meets cellular demand for protein synthesis. Both essential and non-essential amino acids are required by body cells whenever proteins are being synthesized ...
Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids, and the breakdown of proteins (and other large molecules) by catabolism. Dietary proteins are first broken down to individual amino acids by various enzymes and hydrochloric acid present in the gastro-intestinal tract. These amino acids are further broken down to α-keto acids which can be recycled in the body for generation of energy, and production of glucose or fat or other amino acids. This break-down of amino acids to α-keto acids occurs in the liver by a process known as transamination, which follows a bimolecular ping pong mechanism. Protein biosynthesis relies on four processes: amino acid synthesis RNA synthesis transcription translation Protein anabolism is the process by which protein are formed from amino acids (a.k.a. anabolic amino acid synthesis). Protein catabolism is the process by which proteins are broken down to their amino acids. This is also called ...
Amino acids represent a strong signal that positively regulates mTORC1 (reviewed by Guertin and Sabatini, 2007). It was recently shown that leucine, an essential amino acid required for mTORC1 activation, is transported into cells in a glutamine-dependent fashion (Nicklin et al., 2009). Glutamine, which is imported into cells through SLC1A5 [solute carrier family 1 (neutral amino acid transporter) member 5], is exchanged to import leucine via a heterodimeric system composed of SLC7A5 [antiport solute carrier family 7 (cationic amino acid transporter, y+ system, member 5] and SLC3A2 [solute carrier family 3 (activators of dibasic and neutral amino acid transport) member 2]. The mechanism by which intracellular amino acids then signal to mTORC1 remained obscure for many years. The activation of mTORC1 by amino acids is known to be independent of TSC1/2, because the mTORC1 pathway remains sensitive to amino acid deprivation in cells that lack TSC1 or TSC2 (Nobukuni et al., 2005). Some studies have ...
WHAT ARE AMINO ACIDS? Amino acids are the building blocks of protein, and are vital to understanding the Krebs Cycle. They are individual crystalline molecules that make up protein, similar to the way letters make up the alphabet. There are 20 basic amino acids that produce over 1600 substances in the body. They make up 3/4ths of the body s solid material and are found in muscle tissue, organs, blood and skin. Amino acids also make hormones, enzymes, and vitamins, and are essential for a healthy immune system and proper neurological functions. It is necessary to replace amino acids constantly to nourish the body and to repair and regenerate tissue. Amino acids are generally ingested in the food we eat, however, because of processed foods, inadequate diets, and food restrictive programs, a proper balance is rarely achieved and supplementation is advisable. This holds to be true during illness, trauma, surgery and stress. More amino acids are required than can be obtained by food alone. In the chronically
Typical Amino Acid Profile contains: Essential Amino Acids: L-Isoleucine - 317 mg, L-Leucine - 508 mg, L-Lysine - 437 mg, L-Methionine - 166 mg, L-Phenylalanine - 306 mg, L-Threonine - 260 mg, L-Tryptophan - 104 mg; L-Valine - 890 mg; Non-Essential Amino Acids: L-Alanine - 287 mg, L-Arginine - 432 mg, L-Aspartic Acid - 462 mg, L-Cysteine - 45 mg, L-Glutamic Acid - 1,334 mg, L-Glycine - 289 mg, L-Histidine - 133 mg, L-Proline - 629 mg, L-Serine - 333 mg, L-Tyrosine - 263 mg ...
Previous studies showed that maternal high-protein supplementation during human pregnancy results in poor fetal outcomes, including fetal growth restriction. Using late-gestation pregnant sheep, this study aimed to determine responses to prolonged and exogenous fetal amino acid supplementation under normal conditions to understand the mechanisms that might explain how fetal growth is compromised when excess amino acids are delivered chronically to the fetus. The novel findings of this study are that a chronic infusion of mixed amino acids directly into a normally growing sheep fetus did not simply replace placental transport of amino acids to the fetus, as amino acid concentrations and delivery rates into the fetus were maintained or increased. The amino acid infusion increased fetal leucine oxidation but did not affect protein synthesis or accretion rates. Furthermore, there was a decrease in fetal glucose uptake from the placenta, indicating that exogenous amino acids were used as alternative ...
Astymin-SN contains all ESSENTIAL AMINO ACIDS & NON-ESSENTIAL AMINO ACIDS with Xylitol. Astymin-SN is a total Amino acids infusion formulated as per WHO/FAO recommendations. The composition is also in accordance with VUJ-N mixture and human plasma serum concentration.. With the addition of Insulin independent Xylitol, Astymin-SN delivers protein sparing effect. Astymin-SN increases protein synthesis, improves nutritional status and builds body resistance. In conditions of HIGH NITROGEN & PROTEIN NEEDS, Astymin-SN is an ideal formula.. ...
BCAA means branched chain amino acid and it is progressively being acknowledged as an essential supplement within the area of sports diet. Muscleenergy has its own super plus version of the supplement pre workout BCAAs Branched Chain Amino Acid + Vitamin B6. In a nutshell the word describes three proteinogenic amino acids essential Aminos - leucine, isoleucine and valine.. BCCAs are broadly referred to as foundations of protein. When protein meals are eaten it will get digested into individual proteins and short chains of proteins which are sufficiently little to become made available to the blood stream. Theyre then utilized by your body to construct and repair tissue among other activities.. Amino acids are organic compounds that contain two groups of molecules: amino (-NH2) and carboxyl (-COOH). There are a total of 19 amino acids in the human diet, of which 11 are non-essential, and the remaining 8 are essential. It is this critically important fact that there are 2 kinds of amino acids -- ...
Amino acids are needed for a multitude of purposes in the human body on a constant basis. Non-essential amino acids are manufactured within the body and can be ordered by the brain "on the spot". Essential amino acids must come from the foods that we eat.. If we do not receive enough of them through the foods we take in, then our bodies must find them in existing protein structures, mainly the muscles. If the brain senses the need to metabolise certain protein molecules in order to fuel necessary activities, then the muscle tissue will be metabolised, regrouped and used as needed.. How can I avoid protein catabolism?. There are several methods to employ in order to avoid the onset of protein catabolism. Especially for athletes, but for all others as well, we need our protein! Maintaining solid muscle mass throughout life increases resting metabolism rates, enables us to thrive in our later years, makes us confident and enhances all of life in general.. ...
Cutting out certain amino acids - the building blocks of proteins - from the diet of mice slows tumor growth and prolongs survival, according to new research published in Nature. Researchers at the Cancer Research UK Beatson Institute and the University of Glasgow found that removing two non-essential amino acids -…
Tetrahydrobiopterin (BH4) is a naturally occurring cofactor essential for critical metabolic pathways. Studies suggest that BH4 supplementation may ameliorate autism symptoms; the biological mechanism for such an effect is unknown. To help understand the relation between central BH4 concentration and systemic metabolism and to develop a biomarker of central BH4 concentration, the relationship between cerebrospinal fluid BH4 concentration and serum amino acids was studied. BH4 concentration was found to be distributed in two groups, a lower and higher BH4 concentration group. Two serum amino acids, citrulline and methionine, differentiated these groups, and the ratio of serum citrulline-to-methionine was found to correlate with the cerebrospinal fluid BH4 concentration (r = -0.67, p
Stress hormones were infused for 6 h in healthy volunteers (n = 32). Free amino acid concentrations were determined in plasma and in skeletal muscle biopsy specimens. A triple hormone combination of adrenaline, cortisol, and glucagon raised the level
A new method for the determination of amino acids is presented. It combines established methods for the derivatization of primary and secondary amino groups with 9-fluorenylmethoxycarbonyl chloride (Fmoc-Cl) with the subsequent amino acid specific detection of the derivatives by LC-ESI-MS/MS using multiple reaction monitoring (MRM). The derivatization proceeds within 5 min, and the resulting amino acid derivatives can be rapidly purified from matrix by solid-phase extraction (SPE) on HR-X resin and separated by reversed-phase HPLC. The Fmoc derivatives yield several amino acid specific fragment ions which opened the possibility to select amino acid specific MRM transitions. The method was applied to all 20 proteinogenic amino acids, and the quantification was performedusing l-norvaline as standard. A limit of detection as low as 1 fmol/μl with a linear range of up to 125 pmol/μl could be obtained. Intraday and interday precisions were lower than10 % relative standard deviations for most of the ...
A robust system for the preparation of β-heteroaryl α-amino acid derivatives has been developed using photoredox catalysis. This system operates via regiospecific activation of halogenated pyridines (or other heterocycles) and conjugate addition to dehydroalanine derivatives to deliver a wide range of unnatu
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Protein Powder (Digestive). What is protein? Protein is an essential nutrient for the human body, and the building blocks of body tissue.  Protein is made up of several amino acids: essential, and non-essential.  Non-essential amino acids are readily manufactured in our liver, and these comprise approximately 80% of the amino acids.  The essential amino acids are the remaining 20%, and we can only get them from our diet, or in supplement form.  Available in Whey or Vegan sources.
Mild excess of amino acids will do little damage ( it would be far worse to eat a 16 ounce steak ). Large amounts of particular amino acids could stress your system and your kidneys. The largest damage might be to your wallet. Many companies sell products that are very expensive on a $/pound basis. The products have merit, and are generally safe and effective, but cost a lot. My personal preference is to take drinks with amino acids during the run, take a few specific aminos after a long run, and then follow it up with real food, like a cheeseburger or a good dinner. I.E. I like specialized products just before, during and just after a run, but use real food all the rest of the time. Karl King ( who has financial interest in some of the type of products mentioned ) ...
Protein Powder (Endurance). What is protein? Protein is an essential nutrient for the human body, and the building blocks of body tissue.  Protein is made up of several amino acids: essential, and non-essential.  Non-essential amino acids are readily manufactured in our liver, and these comprise approximately 80% of the amino acids.  The essential amino acids are the remaining 20%, and we can only get them from our diet, or in supplement form.  Available in Whey or Vegan sources.
Veal is a promising raw material for use in the daily diet, as well as for production of functional and dietary foods. However the effect of cold treatment on the amino acid composition of veal has not been sufficiently studied. The aim of this study was the amino acid composition analysis of veal subjected to various variants of cold treatment. The selected material under research was muscle tissue of hip parts from calves, grown in the Leningrad Region, Russia and aged no more than 3 months. Cooling to 4 ± 1°C and rapid freezing to the temperature of minus 18°C at the cooling air temperatures of minus 24°C and minus 35°C were used as variants of cold treatment. Amino acid composition analyses were carried out using precolumn derivatization with phenylisothiocyanate and reversed-phase gradient HPLC on the Shimadzu 20-AD chromatograph with spectrophotometric detection at 254 nm. The results show the effect of cold treatment on the content of free amino acids and total amino acid composition ...
All purpose seasoning from soy protein. Natural soy sauce alternative. Gluten-free. Contains no preservatives. Non GMO project verified. nongmoproject.org. Serving health worldwide since 1912. 3 John 2. 1912-2012. Celebrating 100 years. Patricia Bragg - N.D., Ph.D., Pioneer Health Crusader, Health Educator, Author. Paul C. Bragg - N.D., Ph.D., Originator Health Stores, Life Extension Specialist. Bragg Liquid Aminos is a vegetable protein seasonings from healthy, certified non-GMO soybeans from the original formula by Health Pioneer and the originator of Health Stores, Paul C. Bragg. Bragg Liquid Aminos. Gourmet alternative to tamari & soy sauce. No preservatives. No alcohol. Not fermented. Contains the Following 16 Amino Acids: alanine, arginine, aspartic acid, glutamic acid, glycine, histidine, isoleucine, lysine, leucine, methionine, phenylalanine, proline, serine, threonine, tyrosine, valine. 16 essential & non-essential amino acids in naturally occurring amounts from liquid non-GMO soy ...
Asparagine. Molecular model of the amino acid asparagine. Its chemical formula is C4.H8.N2.O3. Atoms are represented as spheres and are colour- coded: carbon (blue), hydrogen (gold), oxygen (red) and nitrogen (dark blue). Amino acids are the building blocks of proteins. Asparagine is a non-essential amino acid. It can be synthesised by the body and so does not need to come from the diet. Asparagine plays an important role in the folding of protein molecules into their secondary structures (alpha helices and beta sheets). Some proteins (such as haemoglobin, the oxygen- carrying pigment in human blood) cannot function without being folded into the correct shape. - Stock Image A611/0042
Amino Acid Metabolism Student Edition 6/3/13 version Dr. Brad Chazotte 213 Maddox Hall [email protected] Web Site: http://www.campbell.edu/faculty/chazotte Original material only ©2004-14 B. Chazotte Pharm. 304 Biochemistry Fall 2014 Goals • Understand the relationship of nitrogen to carbon intermediary metabolism. • Learn the Urea Cycle sequence, reactions, and products. • Have an understanding of an overview of amino acid catabolism resulting in 7 basic products and the difference between ketogenic and glucogenic catabolism. • Have an understanding of an overview of amino acid anabolism from basic precursors. • Understand the concept of essential and nonessential amino acids in the diet of humans. • Understand that many diseases can arise from errors in amino acid metabolism. Do NOT memorize any of the specific amino acid catabolic or anabolic pathways. They are for informational purposes only. Nitrogen Pathways in Intermediary Metabolism Plants Matthews et al 2000 Figure 20.1 ...
Proteins are composed of amino acids, and the human body requires 20 such amino acids for its normal growth and development. When considering a protein diet, it is important to know that certain foods carry proteins containing essential amino acids which are NOT produced by the body itself but ARE essential to the bodys processing of the other 12 non-essential amino acids ...
OBJECTIVE: To test the hypothesis that protein metabolism is not totally normalized in insulin treated gestational diabetes mellitus (GDM) patients compared with normal, pregnant control subjects. RESEARCH DESIGN AND METHODS: Protein metabolism in eight Hispanic women with insulin-treated GDM and eight healthy Hispanic control women was studied in late gestation and at 6 weeks postpartum. Nitrogen flux was assessed from the disposal rate of [15N]-labeled urea over 12 h after a dose of [15N]-labeled leucine. Plasma amino acid concentrations were determined in fasting and 2-h postprandial samples using an amino acid analyzer. RESULTS: Protein turnover was normalized in insulin-treated GDM; however, fasting and postprandial plasma amino acids were elevated antepartum and postpartum. Nitrogen flux was significantly lower during pregnancy (P = 0.04-0.001) and did not differ between groups. Fasting and postprandial plasma amino acids were elevated in GDM antepartum and postpartum, despite satisfactory ...
The Bloodspot Amino Acid Test can illuminate problems in amino acid absorption by determining essential amino acid imbalances from a simple finger stick.
Of course, we have all heard about Steel Cut Oats, but what about Quinoa, Millet or Buckwheat? Quinoa was used by the Incas and is still a staple food in South America. This whole grain is a complete protein grain and contains the following essential amino acids: Isoleucine, Leucine, Lysine, Phenylalanine, Methionine, Threonine, Tryptophan and Valine. In addition, Quinoa includes the following non-essential amino acids Cystine and Tyrosine. One serving (1/3 cup) supplies only 134 calories and 3 gms fiber, 4 gms of complete protein and 23 gms of complex carbs to give you the energy you need to burn fat ...
Summary Correlation-based network analysis (CNA) of the metabolic profiles of seeds of a tomato introgression line mapping population revealed a clique of proteinogenic amino acids: Gly, Ile, Pro, Ser, Thr, and Val. Correlations between profiles of these amino acids exhibited a statistically significant average correlation coefficient of 0.84 as compared with an average correlation coefficient of 0.39 over the 16 119 other metabolite cliques containing six metabolites. In silico removal of cliques was used to quantify their ...
Glutamine is the most abundant naturally occurring non-essential amino acid in the body and it can be derived from glutamic acid, another member of the amino acid family. Both glutamine and glutamic acid can be found in protein-rich foods such as red meat, nuts and fish. Different tissues in the body have different requirements for L-Glutamine and the most eager consumers of glutamine are the cells of intestines, whilst muscles are known to be high producers of L-Glutamine.. ...
A serotonin imbalance affects appetite and sleep and can result in lack of appetite and weight loss commonly seen in depression sufferers as well as insomnia or excessive sleepiness (hypersomnia). Furthermore, the amino acid tryptophan helps synthesize melatonin, also known as the sleep hormone. As its name suggests, melatonin regulates sleep-wake cycles, but its synthesis can be affected by a lack of the amino acid in the diet, potentially resulting in a disruption in normal sleeping patters consistent with depression symptoms.. Another example of an amino acid that impacts depression and mental health in general is tyrosine. Tyrosine is a non-essential amino acid and its found in a variety of high protein foods such as beef, pork, turkey, chicken, fish, eggs, milk, cheese and plant-based sources of protein such as legumes, pumpkin seeds, sesame seeds etc. In other words, it is pretty easy to meet your daily requirements and, in case you dont, the human body can synthesize it from other ...
... nm was 1.145. The protein content of that solution, calculated from quantitative amino acid analysis, was 256 micrograms/mL. Calculate the extinction coefficient of the protein in unitsbof mL/mg/cm. Assume that the molecular mass of the protein was 13,000. Calculate the molar extinction coefficient. ...
GABA is a non-essential amino acid. It plays an essential role in balancing brain chemicals. Learn all about the various health benefits of GABA
Glutamic acid. Molecular model of the non-essential amino acid glutamic acid (C5.H9.N.O4). This dicarboxylic acid is one of the amino acids that is a precursor to proteins. It is also an important neurotransmitter. Atoms are represented as spheres and are colour-coded: carbon (grey), hydrogen (white), nitrogen (blue) and oxygen (red). Illustration. - Stock Image F016/9771
Most people, no matter their fitness level, take daily vitamin or mineral supplements. But what about amino acids or Branched-chain Amino Acids (BCAAs
Free Form Amino Acid capsules, provided by Douglas Laboratories, contain a nutritionally balanced mixture ofessential, conditionally essential, and important non-essential amino acids in their physiological L-crystallineforms.FUNCTIONSAmino acids have many functions in the body.
BCHM 501 BIOCHEMISTRY I 3 credits Studies the structures and functions of proteins and enzymes such as amino acids and peptides; the metabolism of carbohydrates and lipids, the respiratory chain, oxidative phosphorylation, citric acid cycle, glycolysis, ketogenesis and the synthesis of cholesterol. Included are the biosynthesis of essential and non-essential amino acids and the catabolism of amino acids. Prerequisite: Biology and Chemistry. ...
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.
Bragg Liquid Aminos is a non-GMO Project Verified liquid protein concentrate, derived from soybeans. It contains 16 naturally-occuring essential and non-essential amino acids.
Each capsule supplies: Glutamine (as L-Glutamine)* . . . . . . . . . . . . . . . . . . . . . . . . . . . 500 mg*Nonhydrolyzed, naturally produced, free-form L-Amino Acid RECOMMENDATION: One (1) capsule one (1) to three (3) times each day as a dietary supplement or as otherwise directed by a healthcare professional. Contains: 180 Capsules L-Glutamine - one of the non-essential amino acids, glutamine is a major fuel for enterocytes, and supports tissues that turn over rapidly, such as intestinal cells (intestinal epithelium) and componentsof the immune system.
Tyrosine (Tyr, Y) or 4-hydroxyphenylalanine is a non-essential amino acid with a polar side group. Its codons are UAC and UAU. Aside from being a proteogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes. It functions as a receiver of phosphate groups that are transferred by way of protein kinases (so-called receptor tyrosine kinases). Phosphorylation of the hydroxyl group changes the activity of the target protein. (Wikipedia) L-Tyrosine is the enantiomer of tyrosine (the other being D-tyrosine) that is used in building proteins ...
Up-to-date, the preterm newborn nutrition is based on human breast milk or its imitations. However, the growth rate is known to be reduced compared to the fetal growth rate. In order to attempt a better growth rate of the preterm newborn infants it is important to evaluate the metabolic components of the fetal blood and try to find components that might influence its growth.. Little is known of the metabolic components of the fetal blood, including amino acid profile. The aim of the study is to evaluate amino acid profile in the fetus blood in different gestational ages and compare it to post natal period. ...
Risk Information: Consult a health care practitioner prior to use if you are pregnant or breast feeding or following a low protein diet. Keep out of reach of children.. Tyrosine is a precursor (a preceding part of a biological process) of the neurotransmitters norepinephrine and dopamine, which regulate moods, among other things. Tyrosine is a non-essential amino acid, meaning that the body normally produces it. It acts as a mood elevator: conversely, a lack of adequate amounts of tyrosine leads to a deficiency of norepinephrine in the brain, which in turn can result in depression. Extra amounts of tyrosine in the diet may elevate brain levels of norepinephrine, improving neurotransmissions and doing away with depression.. Research into causes of organic depression continues. Vitamins B1, B6, phenylalanine in L, and DL forms, tyrosine, tryptophan and other psycho-chemicals are showing some notable benefits. However, because we humans are infinitely complicated, we cant possibly expect to find ...
Foods with amino acids are the building blocks of protein. That means they are responsible for strength, repair and rebuilding inside your body. Your tissues, your cells, your enzymes and your brain all get their nourishment and protection from amino acids.. Why You Need Amino Acids Daily. Amino acids make up 75% of the human body, and are vital to every part of human function. One of the most talked about properties of amino acids is how it can assist in muscle building. Amino acids are boasted as the key ingredients in many body-building supplements, though the degree of success they achieve in that form is debatable. Careful attention to amino acids isnt just for people who want to build muscle. Different studies have linked amino acid balances with fighting everything from depression to Fibromyalgia. You Cant Store Amino Acids. The problem with amino acids is that they deteriorate. The body will store extra starch and protein as fat, to use later. Amino acids are not stored, but they can ...
At rest, arterial FFA concentration as well as FFA release was higher in CHF than in controls (p , 0.05 and ,0.001, respectively). During exercise the difference in FFA release between CHF and controls declined but remained significant (p , 0.01). At rest, blood femoral vein was acidotic in CHF (pH = 7.34 ± 0.02 vs. 7.41 ± 0.01 in controls; p , 0.05); during the effort, the pH of CHF further decreased (7.31 ± 0.01; p , 0.01).. This investigation shows that patients with CHF exercising at a light workload have a net muscle release of both Phe and other amino acids. The mechanisms responsible for the net release of Phe during exercise in CHF patients may include alterations in intermediary and energy metabolism within muscle cells, intracellular acidosis, and cytokine production. Indeed, the low intramuscular glycogen concentration in resting CHF patients (4) may make muscle energy metabolism more dependent on alternative substrates such as amino acids derived from cellular-free pool and/or ...
Using bacterial genomes that have been entirely recoded, Yale scientists have developed a way to induce cells to produce novel protein-based polymers that can be used for new materials and therapeutics.. Cells usually assemble proteins using 20 amino acids and scientists have found it difficult to incorporate synthetic amino acids in more than a single or few positions in proteins. The new technology, described Nov. 16 in the journal Nature Biotechnology, shows how it is possible to incorporate many new synthetic amino acids into proteins and thus go beyond the standard 20 building blocks to endow completely new function.. No longer will scientists be limited in the quantity and diversity of novel amino acids they can use to make new therapeutics and materials in bacterial factories, the authors say.. "Now we can introduce dozens of new synthetic building blocks with user-defined precision and at will - as many times as we want - to produce new compounds to improve drugs or functionalized ...
Maddocks ODK, Nature, The non-essential amino acids serine and glycine are used in multiple anabolic processes that support cancer cell growth and proliferation (reviewed i
... Solaray. Combination of these two non-essential amino acids in a 500mg l-arginine and 250mg Ornithine ratio.
Culture isolated ICMs on a feeder layer of mitotically inactivated mouse embryonic fibroblasts plated on gelatin-coated tissue culture plates. Culture medium: Knockout DMEM, supplemented with KO-Serum Replacement (8% or 10%), Plasmanate (8% or 10%), fetal calf serum (5%), Glutamax-I (2 mM), non-essential amino acids (1%), penicillin (50 U/ml) and streptomycin (50 ug/mL), beta-mercaptoethanol (0.055mM), recombinant hLIF (12ng/mL), and bFGF (5ng/mL). Mechanically dissociate ICM-like clumps 6 to 10 days after the initial plating, and replate on fresh feeder layers. Cells can be cryopreserved in freezing media consisting of FCS (90%) and DMSO (10%). Cryopreservation in hES culture media plus DMSO (10%) results in similar yield upon thawing.. ...
L-Tyrosine is a non-essential amino acid that can be synthesized by the body. It can be used to regulate mood and stimulate the nervous system. Its a...
L-cys | L-cysteine antibody, cytesteine antibodies, AS08 360Cysteine (a non-essential amino acid) is a building block of antioxidant glutathione. With a thiol side chain, cysteine is an important structural and functional component of many proteins and en
Using high performance liquid chromatographic method, for the first time, this study determined the concentrations of 17 serum amino acids of the Yangtze finless porpoise (Neophocaena phocaenoides asiaeorientalis) in Tian-e-zhou Baiji Nature Reserve and the Baiji Dolphinarium of Institute of Hydrobiology, Chinese Academy of Sciences. The results showed that the mean concentrations of 14 serum amino acids (Aspartic acid Asp, Glutamic acid Glu, Serine Ser, Arginine Arg, Glycine Gly, Threonine Thr, Alanine Ala, Isoleucine Ile, Leucine Leu, Phenylalanine Phe, Valine Val, Lysine Lys, Tyrosine Tyr and Cysteine Cys) of captive porpoises were significantly higher (p < 0.0001 or 0.05) than those of free-ranging animals, except for Proline Pro, Methionine Met and Histidine His. No significant differences of serum amino acid concentrations were noted between genders and between mature and immature free ranging Yangtze finless porpoises. Glu of captive Yangtze finless porpoise was the highest, then was the ...
Heliconius and Laparus butterflies exhibit a unique pollen-collecting behaviour that enhances lifespan and fecundity. The specific nutritional contribution of pollen, however, had not been previously demonstrated. We used stable isotope variation to trace the carbon flow into eggs from corn pollen provided experimentally to ovipositing female Heliconius charitonia, and to evaluate the use of isotopically contrasting nectar sugars in egg amino acids. The δ13C of individual amino acids from pollen, larval host plant and the eggs from experimental butterflies was measured with gas chromatography/combustion/isotope ratio mass spectrometry (GC/C/IRMS), to evaluate amino acid transfer. The δ13C of egg essential amino acids indicated a transfer of essential amino acids from pollen to butterfly eggs. However, the δ13C of non-essential amino acids reflected the isotopic composition of the artificial nectar, indicating that H. charitonia synthesizes non-essential amino acids from dietary sugars. This, ...
Previously, we developed a novel production technique for giant masu salmon (GMS). This study aimed to develop a fish sauce from GMS to explore ways to efficiently utilize the salmon and to enrich the fish sauce with γ-aminobutyric acid (GABA) by microbial fermentation. The minced bodies of GMS were autolyzed by endogenous protease at 55 °C and 60 °C. During autolysis, the changes in total free amino acids and protein size was monitored by LC-MS and SDS-PAGE analysis, respectively. After 96 h, fish sauce was prepared by heating, and the amino acid composition was analyzed by LC-MS. To enrich the fish sauce with GABA, Lactobacillus plantarum strain N10 was added and incubated at 28 °C for 48 h. The total free amino acids content significantly increased for 96 h. SDS-PAGE analysis showed that major bands at 200 kDa and 48 kDa detected at 0 h gradually disappeared over time. The ratio of anserine to total amino acids in the fish sauce was approximately 36%. The concentration of GABA in
The δ15N values of organisms are commonly used across diverse ecosystems to estimate trophic position and infer trophic connectivity. We undertook a novel cross-basin comparison of trophic position in two ecologically well-characterized and different groups of dominant mid-water fish consumers using amino acid nitrogen isotope compositions. We found that trophic positions estimated from the δ15N values of individual amino acids are nearly uniform within both families of these fishes across five global regions despite great variability in bulk tissue δ15N values. Regional differences in the δ15N values of phenylalanine confirmed that bulk tissue δ15N values reflect region-specific water mass biogeochemistry controlling δ15N values at the base of the food web. Trophic positions calculated from amino acid isotopic analyses (AA-TP) for lanternfishes (family Myctophidae) (AA-TP ~2.9) largely align with expectations from stomach content studies (TP ~3.2), while AA-TPs for dragonfishes (family Stomiidae)
Previous neurochemical and behavioural studies show that tyrosine depletion using a nutritionally balanced tyrosine-free amino acid mixture attenuates the dopamine-releasing and psychostimulant properties of amphetamine. Here we investigate the effect of a tyrosine-free amino acid mixture on striatal binding of [(11)C]raclopride, and amphetamine-induced [(11)C]raclopride displacement, using positron emission tomography in the rat. Rats were scanned for 60 min after an i.v. injection of approximately 11 MBq [(11)C]raclopride using a quad-HIDAC system. Amphetamine (2 mg/kg i.p., 30 min prior to scan) caused a 12% reduction in [(11)C]raclopride distribution volume ratio (DVR) compared to saline-injected controls. The tyrosine-free amino acid mixture (1 g/kg i.p.) caused a small (+7%) but statistically insignificant increase in [(11)C]raclopride DVR and attenuated, although it did not fully block, the amphetamine-induced reduction. These data are in keeping with previous neurochemical, immunocytochemical,
AGHAKHANIAN, F.; ZAREI, A.; LOTFOLLAHIAN, H. y EILA, N.. Apparent and true amino acid digestibility of artemia meal in broiler chicks. S. Afr. j. anim. sci. [online]. 2009, vol.39, n.2, pp.158-162. ISSN 2221-4062.. In order to determine the amino acid digestibility of artemia meal, five-week old male broiler chicks were given a semi-purified diet in which artemia meal was the sole source of protein. Apparent amino acid digestibility values of the assay diet, using ileal and excreta contents, were calculated using chromic oxide as indigestible marker. True digestibility values were calculated using endogenous output determined by feeding a nitrogen-free diet. The results showed that in determination of apparent amino acid digestibility of excreta, serine had the lowest (0.80) and methionine the highest (0.92) digestibility, while glycine had the lowest (0.88) and arginine and leucine the highest (0.95) apparent ileal digestibility. In measuring true excreta and ileal amino acid digestibility, ...
Groups of rats were deprived of food overnight and then given free access to diets designed to raise (carbohydrate) or lower (carbohydrate and large neutral amino acids) brain tryptophan concentrations. Similar diets were supplemented with 40% fat and fed to other groups. All animals were killed 2h after food presentation. Sera from animals fed carbohydrate plus fat contained 2.5 times as much free tryptophan concentrations did not differ. Similarly, sera from rats fed on carbohydrate, large neutral amino acids, and 40% fat contained 5 times as much free tryptophan as those from rats given this meal without fat, but brain tryptophan concentrations increased by only 26%. Correlations were made between brain tryptophan and (1) free serum tryptophan, (2) the ratio of free serum tryptophan to the sum of the other large neutral amino acids in serum that compete with it for uptake into the brain, (3) total serum tryptophan or (4) the ratio of total serum tryptophan to the sum of its circulating ...
Frailty is a clinical entity associated with an increase in risk for disease and death and becomes more common as people age. Frailty has a strong relationship with the age-related loss of muscle and strength, termed sarcopenia. Sarcopenia and frailty are strongly associated with disability, especially in women. Adequate protein intake, the amino acid leucine, and resistance exercise training have been individually shown to increase muscle mass to varying degrees. However, no studies have investigated how a longer-term resistance exercise training program with leucine supplementation when protein intake is optimized could increase muscle mass in frail and pre-frail elderly women. In addition, this is the population that stands the most to gain from such an intervention.. The purpose of this study is to investigate the effects of the amino acid leucine added to resistance exercise training on muscle mass and physical performance in frail and pre-frail elderly women with adequate protein intake. ...
Looking for online definition of branched-chain amino acids in the Medical Dictionary? branched-chain amino acids explanation free. What is branched-chain amino acids? Meaning of branched-chain amino acids medical term. What does branched-chain amino acids mean?

Amino Acid Solutions by B Braun Medical | Medline Industries, Inc.Amino Acid Solutions by B Braun Medical | Medline Industries, Inc.

Standard Amino Acids are available in 10% and 15% concentrations. Specialty Amino Acids include: TrophAmine®: (6% and 10% amino ... Amino Acid Solutions by B Braun Medical. B. Braun offers a wide selection of specialty and standard amino acids formulations, ... FreAmine HBC®: (6.9% amino acids injection) Parenteral nutrition solution containing 45% BCAA and indicated for the support of ... NephrAmine®: (5.4% essential amino acids injection) Parenteral nutrition solution for the acute and chronic renal failure ...
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Fructosyl amino acid oxidase Research Products: Novus BiologicalsFructosyl amino acid oxidase Research Products: Novus Biologicals

Browse our Fructosyl amino acid oxidase product catalog backed by our Guarantee+. ... Fructosyl amino acid oxidase products available through Novus Biologicals. ...
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Health Library - C573 - Branched Chain Amino Acids (BCAAs) - Natural, Alternative - 21527Health Library - C573 - Branched Chain Amino Acids (BCAAs) - Natural, Alternative - 21527

... 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 ...
more infohttp://healthlibrary.epnet.com/GetContent.aspx?token=e0498803-7f62-4563-8d47-5fe33da65dd4&chunkiid=21527

SLC3: Heavy Subunits of the Heteromeric Amino Acid Transporter Family Research Areas: R&D SystemsSLC3: Heavy Subunits of the Heteromeric Amino Acid Transporter Family Research Areas: R&D Systems

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 ...
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Branched-chain amino acids ForumBranched-chain amino acids Forum

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 ...
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METHOD OF PRODUCING OPTICALLY ACTIVE N-(HALOPROPYL) AMINO ACID DERIVATIVE - Patent applicationMETHOD OF PRODUCING OPTICALLY ACTIVE N-(HALOPROPYL) AMINO ACID DERIVATIVE - Patent application

... examples of acids to be used include hydrochloric acid, sulfuric acid, hydrobromic acid, acetic acid, toluenesulfonic acid, ... amino acid derivative. BACKGROUND ART [0002] Optically active N-(halopropyl)amino acid derivatives are used for, for example, ... The amino acid derivative represented by formula (IV) can be used for the synthesis of optically active cyclic amino acids. ... amino acid derivative.. Claims:. 1. A method for producing an optically active N-(halopropyl)amino acid derivative, comprising ...
more infohttp://www.patentsencyclopedia.com/app/20110190527

Entropy | Free Full-Text | Glyphosates Suppression of Cytochrome P450 Enzymes and Amino Acid Biosynthesis by the Gut...Entropy | Free Full-Text | Glyphosate's Suppression of Cytochrome P450 Enzymes and Amino Acid Biosynthesis by the Gut...

... we show how interference with CYP enzymes acts synergistically with disruption of the biosynthesis of aromatic amino acids by ... Samsel, A.; Seneff, S. Glyphosates Suppression of Cytochrome P450 Enzymes and Amino Acid Biosynthesis by the Gut Microbiome: ... Samsel A, Seneff S. Glyphosates Suppression of Cytochrome P450 Enzymes and Amino Acid Biosynthesis by the Gut Microbiome: ... Glyphosates Suppression of Cytochrome P450 Enzymes and Amino Acid Biosynthesis by the Gut Microbiome: Pathways to Modern ...
more infohttp://www.mdpi.com/1099-4300/15/4/1416

Global Feed Amino Acids Market | Growth, Market Share, and Forecast to 2022Global Feed Amino Acids Market | Growth, Market Share, and Forecast to 2022

Feed Amino Acids Market report is categorized by Livestock (Poultry, Aquaculture, Ruminants, Swine), Form (Liquid, Dry), Type ( ... Figure 1 Feed Amino Acids Market Segmentation. Figure 2 Feed Amino Acids: Livestock Segmentation. Figure 3 Feed Amino Acids ... Feed Amino Acids Market, By Livestock & Country 4.4 Feed Amino Acids Market, By Livestock & Region 4.5 Feed Amino Acids Market ... Table 18 Feed Amino Acids for Poultry Market Size, By Region, 2015 2022 (KT). Table 19 Feed Amino Acids for Swine Market Size, ...
more infohttps://www.marketsandmarkets.com/Market-Reports/feed-amino-acids-market-116585197.html

Amino acid synthesis - WikipediaAmino acid synthesis - Wikipedia

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 ...
more infohttps://en.wikipedia.org/wiki/Amino_acid_synthesis

D-Amino acid - WikipediaD-Amino acid - Wikipedia

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 ...
more infohttps://en.wikipedia.org/wiki/D-amino_acids

amino acids Archives - ExtremeTechamino acids Archives - ExtremeTech

If this is indeed the case, it in turn suggests that these wandering amino acids may have played a vital role in the synthesis ... The new-found presence of this complex organic molecule, iso-propyl cyanide, is a good indicator that amino acids themselves ... have discovered large quantities of organic molecules at the center of the Milky Way that resemble life-bearing amino acids in ...
more infohttps://www.extremetech.com/tag/amino-acids

amino acid | FactMonsteramino acid | FactMonster

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 ...
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Amino Acid | Encyclopedia.comAmino Acid | Encyclopedia.com

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 ...
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Amino Acids and Protein SequencesAmino Acids and Protein Sequences

The protein primary structure conventionally begins at the amino-terminal (N) end and continues until the carboxyl-terminal (C ... Each protein or peptide consists of a linear sequence of amino acids. ... Amino Acid Composition and Analysis. The unordered composition of an amino acid is often useful information when attempting to ... There are two main steps to determine the frequency of amino acids in a process known as amino acid analysis. Firstly, ...
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Amino acid - Everything2.comAmino acid - Everything2.com

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 ...
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Clipart - Glutamine (amino acid)Clipart - Glutamine (amino acid)

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. ...
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Glutamine | amino acid | Britannica.comGlutamine | amino acid | Britannica.com

... 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 ...
more infohttps://www.britannica.com/science/glutamine

Cysteine | amino acid | Britannica.comCysteine | amino acid | Britannica.com

... another amino acid. The bonded sulfur atoms form a disulfide bridge, a principal factor in the shape and function of skeletal ... Sulfur-containing nonessential amino acid. In peptides and proteins, the sulfur atoms of two cysteine molecules are bonded to ... Sulfur amino acids such as cysteine are formed by adding sulfhydryl groups and amino groups. Other biosynthesis pathways lead ... amino acid: Cysteine oxidation. The thiol (sulfur-containing) group of cysteine is highly reactive. The most common reaction of ...
more infohttps://www.britannica.com/science/cysteine

Amino Acids - GlycineAmino Acids - Glycine

The Biology Project , Biochemistry , The Chemistry of Amino Acids. Close window Glycine G (Gly). Chemical Properties:. ... The Biology Project , Biochemistry , The Chemistry of Amino Acids. The Biology Project Department of Biochemistry and Molecular ... Glycine is the smallest of the amino acids. It is ambivalent, meaning that it can be inside or outside of the protein molecule ... For example, glycine is a derivative of acetic acid, and the pKa of acetic acid is well known. Alternatively, glycine could be ...
more infohttp://www.biology.arizona.edu/biochemistry/problem_sets/aa/glycine.html

Chromatographic Separation of Amino Acids | SpringerLinkChromatographic Separation of Amino Acids | SpringerLink

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 ...
more infohttps://link.springer.com/chapter/10.1007%2F978-3-030-06082-4_4

separation of pth-amino acidsseparation of pth-amino acids

... 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. ...
more infohttp://www.bio.net/bionet/mm/proteins/1995-January/002093.html

Desalination Research Papers: Amino acidsDesalination Research Papers: Amino acids

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 ...
more infohttps://www.lenntech.com/cgi-bin/abstracts.cgi?t=Amino%20acids

Amino acid metabolism - ConservapediaAmino acid metabolism - Conservapedia

... the transfer of their amino group to an α-keto acid to yield the α-keto acid of the original amino acid and a new amino acid, ... Two nonspecific amino acid oxidases, L-amino acid oxidase and D-amino acid oxidase, catalyze the oxidation of the L- and D- ... Amino Acid Biosynthesis. Biosynthesis of the Nonessential Amino Acids. Biosynthesis of the Essential Amino Acids. Nitrogen ... Amino Acid Deamination. The first reaction in the breakdown of an amino acid is almost always removal of its α-amino group with ...
more infohttp://www.conservapedia.com/Amino_acid_metabolism

Amino Acid Amino AcidAmino Acid Amino Acid

Buy Amino Acid Amino Acid products including Amino Acid Standard (AccQ-Tag, Pico-Tag, AccQ-Tag Ultra) - WAT088122, AccQ-Tag ... Pico Tag™ Amino Acid Analysis of Physiologic Amino Acids, Free Amino Acid Chemistry All-inclusive Package includes: column ... is the most widely used technique for HPLC amino acid analysis. Used for Pico Tag® amino acid analysis of physiologic amino ... is the most widely used technique for HPLC amino acid analysis. Used for Pico Tag® amino acid analysis of physiologic amino ...
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N-acetyl-amino acid (CHEBI:21575)N-acetyl-amino acid (CHEBI:21575)

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 ...
more infohttps://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI%3A21575
  • In addition to these 20, scientists have synthesized more than 70 artificial amino acids that are not found in animals, and more than 100 less common amino acids also occur in biological systems, particularly in plants. (factmonster.com)
  • Each of the common amino acids has, in addition to its chemical name, a more familiar name and a three-letter abbreviation that frequently is used to identify it. (encyclopedia.com)
  • In 1806, French chemists Louis-Nicolas Vauquelin and Pierre Jean Robiquet isolated a compound in asparagus that was subsequently named asparagine, the first amino acid to be discovered. (wikipedia.org)
  • Some amino acids are prone to racemization, one example being lysine , which racemizes via formation pipecolic acid . (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)
  • The key elements of an amino acid are carbon , hydrogen , oxygen , and nitrogen , though other elements are found in the side-chains of certain amino acids. (wn.com)
  • Consequently, amino acids are also precursors of glucose , fatty acids, and ketone bodies and are therefore metabolic fuels. (conservapedia.com)
  • 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)
  • When you cannot find the amino acid you are looking for, or for additional technical information, please contact your local Sigma-Aldrich Office. (sigmaaldrich.com)
  • Two enzymes convert L-amino acids to D-amino acids. (wikipedia.org)
  • This category includes information on feeding and supplementing protein, amino acids, and enzymes to pets. (dmoztools.net)
  • Humans can not synthesize all of these amino acids. (wikipedia.org)
  • Not all organisms are able to synthesize all amino acids. (wikipedia.org)
  • Of the 20-odd amino acids, there are 8 (or 9 , due to the expert factor ) that the body cannot synthesize for itself. (everything2.com)
  • L-amino-acid oxidases convert L-amino acids to the alpha- ketoacids , which are susceptible to reductive amination. (wikipedia.org)
  • In the alpha amino acids, the amino and carboxylate groups are attached to the same carbon atom, which is called the α-carbon. (phys.org)
  • 4.Briefly explain how hydrophobic amino acids (and the rest) are distributed in the tertiary structure of protein? (scribd.com)
  • 5. Briefly explain with examples how amino acids are classified as hydrophobic or hydrophilic? (scribd.com)
  • The non-polar side chain amino acids are called hydrophobic and the amino acid with uncharged polar side chain is called hydrophilic. (scribd.com)
  • These amino acids are hydrophobic and have no charge on the 'R' group. (scribd.com)
  • Herradon and Seebach (1989) Mono- and Dialkylation of Derivatives of (1R,2S)-2-Hydroxyxyclopentanecarboxylic Acid and -cyclohexanecarboxylic Acid via Bicylic Dioxannes Selective Generation of Three Contiguous Stereogenic Centers on a Cyclohexane Ring, Helv. (freepatentsonline.com)
  • They are formed from an mRNA template in a process called translation, by which genetic information, encoded in the form of nucleic acids, is translated into the amino acids essential for protein synthesis. (newworldencyclopedia.org)
  • On the basis of the obtained results, it is possible to develop technologically accessible electrodialysis of amino acids as well as other biologically active substance desalting from cultured liquids. (lenntech.com)
  • For most naturally-occurring amino acids, this carbon has the L-configuration. (wikipedia.org)
  • About 500 naturally occurring amino acids are known (though only 20 appear in the genetic code) and can be classified in many ways. (wikipedia.org)
  • Since the science of nutrition seems to still be in its infancy , different experts identify between 20 and 29 amino acids. (everything2.com)
  • Because of their biological significance, amino acids are important in nutrition and are commonly used in nutritional supplements, fertilizers, and food technology. (wikipedia.org)