| PC | avoirdupois weight [Lat. pondus civile]; packed cells; paper chromatography; paracortex; parent cell... |
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| PCP | parachlorophenate; patient care plan; pentachlorophenol; 1-(1-phenylcyclohexyl)piperidine; periphera... |
| PLOD | procollagen-lysine 2-oxoglutarate 5-dioxygenase |
| LAP | 1) Leukocyte Alkaline Phosphatase 2) Leucine Amino-Peptidase |
| PEP | peptidase; phospho(enol)pyruvate; peer evaluation program; phosphoenolpyruvate; pigmentation, edema,... |
| PIIINP | N-propeptide of type III procollagen |
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| PIIINP | Procollagen type III aminoterminal peptide |
| P IIIP | Type III procollagen |
| PIIIP | Type III procollagen peptide |
| DP IV | Dipeptidyl Peptidase IV |
| procollagen peptidase | <enzyme> The proteases that remove the terminal extension peptides of procollagen, deficiency of these enzymes leads to dermatosparaxis or Ehlers Danlos syndrome. (18 Nov 1997) |
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| procollagen | <cell biology> Triple helical trimer of collagen molecules in which the terminal extension peptides are linked by disulphide bridges, the terminal peptides are later removed by specific proteases to produce a tropocollagen molecule. (18 Nov 1997) |
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| procollagen aminoproteinase | An extracellular enzyme that participates in the processing of collagen, removing the extension peptide at the amino-terminal end of procollagen. (05 Mar 2000) |
| procollagen carboxyproteinase | An extracellular enzyme that participates in the processing of collagen, removing the extension peptide at the carboxy-terminal end of procollagen. (05 Mar 2000) |
| procollagen C-endopeptidase | <enzyme> Cleaves the carboxyl-terminal propeptides from type I pr; in 1996 determined to be identical to bone morphogenetic protein 1 Registry number: EC 3.4.24.19 Synonym: procollagen c-protease, type I procollagen carboxyl-terminal proteinase, c-proteinase, procollagen, procollagen endopeptidase (carboxy terminal splitting), procollagen c-proteinase, bone morphogenetic protein 1, bone morphogenic protein 1, bmp-1 (26 Jun 1999) |
| procollagen-lysine, 2-oxoglutarate 5-dioxygenase | <enzyme> A mixed-function oxygenase that catalyses the hydroxylation of peptidyllysine, usually in protocollagen, to peptidylhydroxylysine. The enzyme utilises molecular oxygen with concomitant oxidative decarboxylation of the cosubstrate 2-oxoglutarate to succinate. Chemical name: Procollagen-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating) Registry number: EC 1.14.11.4 (12 Dec 1998) |
| procollagen n-endopeptidase | <enzyme> An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the formation of collagen. Absence or deficiency of the enzyme causes accumulation of procollagen which results in the inherited connective tissue disorder--dermatosparaxis. Registry number: EC 3.4.24.14 (12 Dec 1998) |
| procollagen-proline dioxygenase | <enzyme> A mixed-function oxygenase that catalyses the hydroxylation of a prolyl-glycyl-containing-peptide, usually in protocollagen, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilises molecular oxygen with a concomitant oxidative decarboxylation of 2-oxoglutarate to succinate. Chemical name: Procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase Registry number: EC 1.14.11.2 (12 Dec 1998) |
| alkaline D-peptidase | <enzyme> A penicillin-recognizing enzyme from bacillus cereus; has beta-lactamase activity; genbank d86380 Registry number: EC 3.4.99.- Synonym: ADP gene product, alkaline d-stereospecific endopeptidase (26 Jun 1999) |
| aspartyllysine peptidase | <enzyme> From human intestinal brush border; stabilised by zn+2 Registry number: EC 3.4.13.- Synonym: zn-stable aspartyllysine peptidase (26 Jun 1999) |
| C5a peptidase | <enzyme> Streptococcus pyogenes enzyme inactivates complement 5a by cleaving at lysine 68, removing a six-amino acid fragment Pharmacological action: complement inactivators Registry number: EC 3.4.99.- Synonym: streptococcus c5a peptidase, gbs c5a-ase, group b streptococci c5a-ase, scpa protein (26 Jun 1999) |
| matrix processing peptidase | <enzyme> From matrix fraction of rat liver mitochondria; cleaves mitochondrial protein precursors; inhibited by metal chelators and reactived by mn2+; classified as EC 3.4.24.64 Registry number: EC 3.4.24.- Synonym: mitochondrial processing peptidase, mitochondrial processing protease, alpha-mpp, beta-mpp, p-52 protein, rat, p-55 protein, rat, mas1 protein, yeast, mas2 protein, yeast (26 Jun 1999) |
| peptidase | <enzyme> Alternative name for a protease. (18 Nov 1997) |
| peptidase D | <enzyme> An enzyme cleaving aminoacyl-l-proline bonds in dipeptides containing a C-terminal prolyl residue; a deficiency of this enzyme results in hyperimidodipeptiduria. Synonym: imidodipeptidase, peptidase D, prolidase. (05 Mar 2000) |
| peptidase P | <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) |
| mitochondrial intermediate peptidase | <enzyme> Removes the octapeptide from the amino terminus of the intermediate protein processed from the protein precursor of certain mitochondrial proteins by the mitochondrial processing peptidase; smip from schizophyllum commune; rmip from rat; ymip from saccharomyces cerevisiae Registry number: EC 3.4.24.59 Synonym: mip peptidase, smip peptidase, rmip peptidase, ymip peptidase (26 Jun 1999) |
| procollagen peptidase |
an endopeptidase that catalyzes the cleavage of specific terminal segments from procollagen chains, specifically used to denote procollagen N-endopeptidase (q.v.) and procollagen C-endopeptidase (q.v.).
출처: www.mercksource.com/pp/us/cns/cns_health_library.j...
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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