Abstract
Procollagen, a precursor of collagen, was isolated from cultured medium of matrix-free cells from tendon of 16-day-old chick embryos. Tendon procollagen was shown, by limited proteolysis with pepsin followed by gel chromatography, to possess collagenase inhibiting capacity at its N- and/or C-terminal additional peptide portion(s). The results suggest that collagenase inhibiting activity is manifested upon conversion of procollagen to collagen to protect it from proteolysis with collagenase.
