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.