| PAL | pathology laboratory; peptidyl-alpha-hydroxyglycine alpha-amidating lysine phase alteration plane; p... |
|---|---|
| PG | paregoric; parotid gland; pentagastrin; pepsinogen; peptidoglycan; Pharmacopoeia Germanica; phosphat... |
| CAP | Cyclophosphamide, Adriamycin(Doxorubicin), cis-Platinum |
| CIS | Carcinoma In Situ |
| PEV | cis-Platinum, Etoposide, Vinblastine |
| PPI | Peptidyl prolyl cis-trans-isomerase |
|---|---|
| PPIase | Peptidyl-prolyl cisltrans isomerase |
| PPIases | Peptidyl-prolyl isomerases |
| 13-cis-RA | 13 cis retinoic acid |
| 9-cis-RA | 9-Cis-retinoic acid |
| peptidyl prolyl cis trans isomerase | See: PPIase and immunophilin. (18 Nov 1997) |
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| cis-9,trans-11-octadecadienoate reductase | <enzyme> Uses NADH and alpha-tocopherol quinol; forms trans-11-octadecenoate Registry number: EC 1.3.1.- Synonym: 9,11-ocdd reductase (26 Jun 1999) |
|---|---|
| cis-trans-isomerases | <enzyme> Enzymes that catalyze the rearrangement of geometry about double bonds. Registry number: EC 5.2 (12 Dec 1998) |
| cis trans test | <molecular biology> The complementation test with two or more interacting genes placed in cis and in trans relationships to each other. A double mutant genome is used in the cis test made from the two single mutant genomes used in the trans test by recombination. If the wild type phenotype is restored by both cis and trans arrangements it is concluded that the two mutations are in different genes and hence that the phenotype is determined by more than one gene. If the trans test is negative and the cis positive this means that the two mutations are in the same gene. If both tests are negative then at least one of the mutations must be dominant. Thus the double test provides a means of fine mapping of genes. A lab test which is used to determine whether two mutations of different genes which affect the same phenotype are on the same functional unit (indicating a cis configuration of the mutated genes) or on different functional units (indicating a trans configuration of the mutated genes). (A functional unit can be a chromosome.) The test is done by mating an individual that has one of the mutations to an individual that has the other one, and observing whether their offspring have the mutant phenotype. If the offspring do not have the mutant phenotype, then the genes are known to be trans, because the offspring have normal copies of each mutant gene on the different functional units which are able to genetically complement each other. If the offspring do have the mutant phenotype, then the genes are known to be cis, because the offspring will always inherit at least one of the mutant genes on the one functional unit, resulting in the mutant phenotype. (09 Oct 1997) |
| 3-carboxy-cis-cis-muconate cyclase | <enzyme> Do not confuse with muconate cycloisomerase Registry number: EC 5.5.1.5 Synonym: 3-carboxy-cis,cis-muconate lactonizing enzyme, 3-cmle, carboxy-cis,cis-muconate cyclase (26 Jun 1999) |
| peptidyl-Asp metalloendopeptidase | <enzyme> Extracellular metalloproteinase secreted by a pseudomonas fragi mutant; partial amino acid sequence given in first source Registry number: EC 3.4.24.33 Synonym: endopeptidase asp-n (26 Jun 1999) |
| peptidyl-dipeptidase A | <enzyme> A hydrolase cleaving C-terminal dipeptides from a variety of substrates, including angiotensin I, which is converted to angiotensin II and histidylleucine. An important step in the metabolism of certain vasopressor agents. It is a chloride-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline. It may also have endopeptidase activity on some substrates. Registry number: EC 3.4.15.1 Synonym: carboxycathepsin, dipeptidyl carboxypeptidase, kinase II, peptidase P. (22 Sep 2002) |
| peptidyl leukotrienes | Leukotrienes having amino acids present (even single amino acids) although not true peptides; e.g., LTC4 is an S-substituted glutathione, LTD4 is an S-substituted cysteinylglycine, LTE4 is an S-substituted cysteine, and LTF4 (also known as gamma-glutamyl-LTE4) is an S-substituted gamma-glutamylcysteine. (05 Mar 2000) |
| peptidyl-Lys metalloendopeptidase | <enzyme> From lysobacter enzymogenes; cleaves at the carboxyl side of lysine residues; active at pH 9;endoproteinase lys-c (EC 3.4.99.30) was combined with EC 3.4.24.20 in 1992 enzyme nomenclature Registry number: EC 3.4.24.20 Synonym: endoprotease lys-c, endopeptidase lys-c, endoproteinase lys-c, lysc protease (26 Jun 1999) |
| prolyl | The acyl radical of proline. Prolyl dipeptidase, an enzyme cleaving l-prolyl-amino acid bonds in dipeptides containing N-terminal prolyl residues. Synonym: iminodipeptidase, prolinase, prolylglycine dipeptidase. Prolyl hydroxylase, an enzyme that catalyses the hydroxylation of certain prolyl residues in collagen precursors using molecular oxygen, ferrous ion, ascorbic acid, and alpha-keotglutarate; a vitamin C deficiency directly affects the activity of this enzyme; one form of this enzyme (prolyl 4-hydroxylase) synthesises 4-hydroxyprolyl residues while another produces 3-hydroxyprolyl residues. (05 Mar 2000) |
| prolyl aminopeptidase | <enzyme> Pepi gene product isolated from lactobacillus delbrueckii Registry number: EC 3.4.11.5 Synonym: proline aminopeptidase, cytosol aminopeptidase v, proline-imino-peptidase, proline iminopeptidase, pro-x aminopeptidase, pepi gene product, pip gene product, xanthomonas (26 Jun 1999) |
| prolyl hydroxylase | Specific proline residues on the amino side of a glycine residue in collagen become hydroxylated at C4, before the polypeptides become helical, by the activity of prolyl hydroxylase. This enzyme has a ferrous ion at the active site and a reducing agent such as ascorbate is necessary to maintain the iron in the ferrous state. The presence of hydroxyproline is essential to produce stable triple helical tropocollagen, hence the problems caused by ascorbate deficiency in scurvy. This unusual amino acid is also present in considerable amounts in the major glycoprotein of primary plant cell walls (see HRGP). (18 Nov 1997) |
| prolyl oligopeptidase | <enzyme> Cleaves dipeptides from n-terminal end of peptide chain if penultimate residue is proline; before 1992 prolyl endopeptidase (thiol-dependent) was EC 3.4.22.18 Registry number: EC 3.4.21.26 Synonym: post-proline cleaving enzyme, proline specific endopeptidase, post-proline endopeptidase, prolyl endopeptidase, proline endopeptidase, prolyl endopeptidase I, prolyl endopeptidase (thiol-dependent) (26 Jun 1999) |
| prolyl T RNA synthetase | <enzyme> Minor descriptor (75-84); on-line and index medicus search amino acyl t RNA synthetases (75-84) Registry number: EC 6.1.1.15 Synonym: l-proline-trna-pro ligase (AMP-forming) (26 Jun 1999) |
| succinylalanyl-alanyl-prolyl-phenylalanyl-7-amino-4-methylcoumarin hydrolase | <enzyme> Enzyme may be involved in attainment of transformed state Registry number: EC 3.4.24.- Synonym: suc-ala-ala-pro-phe-amc hydrolase, saapp-amc-hydrolase (26 Jun 1999) |
| (3-(arginyl)amino-4-(4-nitrophenyl)butyryl)-leucyl-prolyl-threonine | Pharmacological action: neurotransmitters Synonym: 2-afb(p-no2)-proctolin, (afb(p-no2)(2))-proctolin (26 Jun 1999) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|