| PC | avoirdupois weight [Lat. pondus civile]; packed cells; paper chromatography; paracortex; parent cell... |
|---|---|
| PCP | parachlorophenate; patient care plan; pentachlorophenol; 1-(1-phenylcyclohexyl)piperidine; periphera... |
| PLOD | procollagen-lysine 2-oxoglutarate 5-dioxygenase |
| PIIINP | N-propeptide of type III procollagen |
|---|---|
| PIIINP | Procollagen type III aminoterminal peptide |
| P IIIP | Type III procollagen |
| PIIIP | Type III procollagen peptide |
| 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) |
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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) |
|---|---|
| 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 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) |
| 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) |
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