Procollagen: conversion of the precursor to collagen by a neutral protease.
An enzymatic activity (procollagen peptidase), capable of converting the biosynthetic precursor procollagen to collagen at neutral pH, has been identified in rat and chick calvarial bone. Limited proteolysis of procollagen with chymotrypsin resulted in a similar transformation. The activity in bone can be demonstrated in vitro despite inhibition of new collagen synthesis by cycloheximide. Preservation of the collagen precursor in preparations extracted with acetic acid results from inhibition of the enzymatic activity at low pH.
D000818:Animals; D001345:Autoradiography; D001842:Bone and Bones / Q000378:metabolism*; D002642:Chick Embryo; D002845:Chromatography; D003094:Collagen / Q000032:analysis / Q000096:biosynthesis*; D003513:Cycloheximide / Q000494:pharmacology; D005624:Frontal Bone / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D010294:Parietal Bone / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011392:Proline / Q000378:metabolism; D051381:Rats; D014316:Tritium
D014316:Tritium; D003094:Collagen; D003513:Cycloheximide; D011392:Proline; D010447:Peptide Hydrolases