titrate (적정하다
| alpha-amino-beta-ketoadipic acid | 2-Amino-3-oxo-1,6-hexanedioic acid;an intermediate of porphobilinogen synthesis formed by d-aminolevulinic acid synthase from succinyl-CoA and glycine; it rapidly decarboxylates to d-aminolevulinic acid. (05 Mar 2000) |
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| alpha-aminoglutaric acid | <amino acid> One of the 20 _ amino acids commonly found in proteins. Plays a central role in amino acid metabolism, acting as precursor of glutamine, proline and arginine. Also acts as amino group donor in synthesis by transamination of alanine from pyruvate and aspartic acid from oxaloacetate. Glutamate is also a neurotransmitter, the product of its decarboxylation is the inhibitory neurotransmitter amino butyrate (GABA). (18 Nov 1997) |
| alpha-aminoisobutyric acid | 2-amino-2-methylpropionic acid;a synthetic amino acid useful in the study of amino acid transport across cell membranes and in the study of cytokine effects; it is not metabolised by the cell. (05 Mar 2000) |
| alpha-aminosuccinic acid | <amino acid> One of the twenty naturally occurring amino acids. Has the following chemical characteristics: pKa1 pKa2 pKa3 pI Water Solubility (30deg C)2.09-3.86 9.82 2.97 0.6 (09 Oct 1997) |
| alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid hydrolase | <enzyme> Involved in degradation of vitamin b6; forms acetic acid plus ammonia plus carbon dioxide plus alpha-hydroxymethyl-succinic monoaldehyde Registry number: EC 3.5.1.- Synonym: compound b hydrolase (26 Jun 1999) |
| alpha-keto acid dehydrogenase | See: alpha-keto acid dehydrogenase. Anaerobic dehydrogenase, an enzyme (usually a pyridinoenzyme) catalyzing the transfer of hydrogen from some metabolite to some acceptor molecule (e.g., NAD+, cytochrome) other than oxygen; e.g., lactate dehydrogenase's, isocitrate dehydrogenase's, and others in EC class 1, excluding those listed under aerobic dehydrogenase. (05 Mar 2000) |
| alpha-keto acid dehydrogenase complex | See: alpha-keto acid dehydrogenase. Anaerobic dehydrogenase, an enzyme (usually a pyridinoenzyme) catalyzing the transfer of hydrogen from some metabolite to some acceptor molecule (e.g., NAD+, cytochrome) other than oxygen; e.g., lactate dehydrogenase's, isocitrate dehydrogenase's, and others in EC class 1, excluding those listed under aerobic dehydrogenase. (05 Mar 2000) |
| alpha-ketoglutaramic acid | H2N-COCH2CH2COCOOH;a metabolite of glutamine formed by the action of glutamine aminotransferase; elevated in certain cases of hepatocoma. Synonym: 2-oxoglutaric acid. (05 Mar 2000) |
| alpha-ketosuccinamic acid | NH2-CO-CH2-CO-COOH;the transamination product of asparagine; acted upon by ω-amidase. (05 Mar 2000) |
| alpha-(N-acetylaminomethylene)succinic acid hydrolase | <enzyme> Involved in degradation of vitamin b6; forms acetic acid plus ammonia plus carbon dioxide plus succinic monoaldehyde Registry number: EC 3.5.1.- Synonym: compound a hydrolase (26 Jun 1999) |
| alpha-N-acylamino acid hydrolase | <enzyme> Functions in catabolism of n-acetylamino acids resulting from turnover of alpha-n-acetylated proteins Registry number: EC 3.5.1.- Synonym: alpha-n-acetylamino acid hydrolase, anaa-hase, n-acylaminoacyl-peptide hydrolase (26 Jun 1999) |
| Altmann's anilin-acid fuchsin stain | <technique> A mixture of picric acid, anilin, and acid fuchsin which stains mitochondria crimson against a yellow background. (05 Mar 2000) |
| ametriodinic acid | <chemical> 3-acetamido-5-(acetamidomethyl)-2,4,6-triiodobenzoic acid. An ionic monomeric contrast medium. Pharmacological action: contrast media. Chemical name: Benzoic acid, 3-(acetylamino)-5-((acetylamino)methyl)-2,4,6-triiodo- (12 Dec 1998) |
| aminoacetic acid | <amino acid, physiology> The simplest amino acid. It is a common residue in proteins, especially collagen and elastin and is not optically active. It is also a major inhibitory neurotransmitter in spinal cord and brainstem of vertebrate central nervous system. (18 Nov 1997) |
| amino acid | <biochemistry> A class of organic molecules that containing an amino group and can combine in linear arrays to form proteins in living organisms. There are twenty common amino acids: alanine, arginine, aspargine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, and valine. They are key components in all living things from which proteins are synthesised by formation of peptide bonds during ribosomal translation of messenger RNA. All the amino acids have the L configuration, except glycine which is not optically active. Other amino acids occurring in proteins, such as hydroxyproline in collagen, are formed by post translational enzymatic modification of amino acid residues in polypeptide chains. There are also several important amino acids, such as the neurotransmitter y aminobutyric acid, that have no relation to proteins. Amino acids can now be produced by biotechnology in bulk using fermentation and biotransformation. Acronym: AA (13 Nov 1997) |