| 영문 | acetic acid | 한글 | 아세트산, 초산 |
|---|---|---|---|
| 설명 | 분자식은 C2H4O2, 분자량 60.05의 저급 지방산이다. CH3COOH의 구조식을 가진 무색액체로 16.7℃에서 녹고 118.0℃에서 끓는다. 식초의 신맛을 내는 것이고, 농축된 것을 빙초산이라 한다. 상온에서는 액체이며 수용액은 약산성이다. 생체내에서는 일반적으로 아세틸 CoA로 존재하며 아세틸기의 공급원이 되는 외에 지방산이나 스테로이드 등의 생성재료로 중요하다. 아세틸 CoA로부터는 케톤체가 합성되며 조직의 에너지원이 된다. |
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| 영문 | acetylsalicylic acid | 한글 | 아세틸살리실산 |
|---|---|---|---|
| 설명 | 상품명이 아스피린(asprin)인 약. 대표적인 비스테로이드 항염약이다. 즉 항염증(anti-inflammatory), 진통(analgesis), 해열(anti-pyretic)의 효과가 모두 뛰어나지만 위장장애, 과다호흡, 라이증후군(Reye syndrome) 등의 부작용이 있다. |
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| 영문 | uric acid | 한글 | 요산 |
|---|---|---|---|
| 설명 | 결정성의 산. 2, 6, 8-trioxypurine. 화학식은 C5H4N4O3로 사람과 동물의 오줌에서 얻을 수 있다. 핵의 대사산물의 하나. 물, 알콜, 에테르(ether)에는 거의 녹지 않으나 알칼리염의 용액에는 녹는다. 이것의 나트륨염 형태(sodium urate)가 결석의 대부분을 차지한다. 급성백혈병 치료 초기단계와 통풍(Gout)에서 혈중요산이 급격히 오를 수 있다. |
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| 영문 | acid-fast bacillus | 한글 | 항산막대균, 항산균 |
|---|---|---|---|
| 설명 | 아닐린 색소에 염색되기 힘드나 일단 염색되면 강산으로 처리하여도 탈색되지 아니하는 세균을 통틀어 이르는 말. 결해균, 나병균 따위가 있다. |
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| 영문 | acid-fast staining | 한글 | 항산염색 |
|---|---|---|---|
| 설명 | 항산성성질(좀처럼 염색이 되지 않으나 한번 염색이 되면 산성용액에 의해서 탈색이 되지 않는 성질)을 가진 균(예를 들면 결핵균 등)의 검출에 이용되는 염색방법. 방법에는 Ziehl-Neelson법과 Kinyoun법 등이 있다. |
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| BCKD | branched-chain alpha-keto acid dehydrogenase |
|---|---|
| EAA | electroacupuncture analgesia; Epilepsy Association of America; essential amino acid; excitatory amin... |
| AA | abdominal aorta; acetic acid; achievement age; active alcoholic; active assistive [range of motion];... |
| AAN | AIDS-associated nephropathy; alpha-amino nitrogen; American Academy of Neurology; American Academy o... |
| NAA | N-acetyl aspartate; naphthaleneacetic acid; neutral amino acid; neutron activation analysis; neutrop... |
| 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) |
|---|---|
| amino acid activating enzyme | <enzyme> Enzymes catalyzing the formation of a specific aminoacyl-tRNA from an amino acid and adenosine 5'-triphosphate with the concomitant formation of adenosine 5'-monophosphate and pyrophosphate. Synonym: amino acid activating enzyme, aminoacyl-tRNA ligases. (05 Mar 2000) |
| amino acid activation | The first step of protein synthesis, whereby an amino acid reacts with adenosine triphosphate in the presence of aminoacyl RNA synthetase to produce an amino acid adenylate, which provides the energy necessary for the attachment of the amino acid to a specific transfer RNA molecule. (12 Dec 1998) |
| amino acid analysis | Determination and identification of amino acid content of a macromolecule, identification of a specific amino acid in macromolecules, often a mutated protein, identification and quantitation of amino acid content in blood plasma or urine; a key diagnostic aid. (05 Mar 2000) |
| amino acid chloromethyl ketones | <chemical> Inhibitors of serine proteinases and sulfhydryl group-containing enzymes. They act as alkylating agents and are known to interfere in the translation process. Pharmacological action: alkylating agents, protein synthesis inhibitor, serine proteinase inhibitors. (12 Dec 1998) |
| amino acid dehydrogenases | Enzymes catalyzing the oxidative deamination of amino acids to the corresponding oxo (keto) acids; two relatively non-specific varieties exist, l and d, for which l-amino acids and d-amino acids are the respective substrates; the products include NH3 and a reduced hydrogen acceptor (NADH in the l case); amino acid dehydrogenases of greater specificity exist, (e.g., glycine dehydrogenase). Compare: amino acid oxidases. (05 Mar 2000) |
| amino acid isomerases | <enzyme> Enzymes that catalyze either the racemization or epimerization of chiral centres within amino acids or derivatives. Registry number: EC 5.1.1.- (12 Dec 1998) |
| amino acid naphthylamidases | <enzyme> Registry number: EC 3.4.11. (12 Dec 1998) |
| amino acid neurotransmitters | Amino acids released by neurons as intercellular messengers. Among the amino acid neurotransmitters are glutamate (glutamic acid) and gaba which are, respectively, the most common excitatory and inhibitory neurotransmitters in the central nervous system. (12 Dec 1998) |
| amino acid oxidases | Flavoenzymes oxidizing, with O2 and H20, either l-or d-amino acids specifically, to the corresponding 2-keto acids, NH3 and H2O2. Compare: amino acid dehydrogenases, yellow enzyme. (05 Mar 2000) |
| amino acid oxidoreductases | <enzyme> A class of enzymes that catalyze oxidation-reduction reactions of amino acids. Registry number: EC 1.4. (12 Dec 1998) |
| amino acid permease | <enzyme> A widely distributed group of large Integral membrane proteins, required for the entry of amino acids into cells. (18 Nov 1997) |
| amino acid reagent | A reagent used in the identification and quantification of amino acids. (05 Mar 2000) |
| amino acid receptor | <biochemistry> Ligand gated ion channels with specific receptors for amino acid transmitters. An extended protein superfamily that also includes subunits of the nicotinic acetylcholine receptor. (18 Nov 1997) |
| amino acid sequence | The sequence of amino acids as arrayed in chains, sheets, etc., within the protein molecule. This is referred to as the primary structure of proteins. It is of fundamental importance in determining protein conformation. (12 Dec 1998) |