Neutral metallo-proteinases of rabbit bone. Separation in latent forms of distinct enzymes that when activated degrade collagen gelatin and proteoglycans.

摘要

Rabbit bones in culture produce specific collagenase and neutral metallo-proteinase activity in latent forms that can be activated by either 4-aminophenylmercuric acetate or trypsin. Latent neutral metallo-proteinase activity was resolved by gel filtration into two enzymes, distinct from collagenase, that degrade gelatin and cartilage proteoglycans.