Purification and properties of a collagenase inhibitor from cultures of bovine aorta.

Bovine medial explants in culture synthesize a potent inhibitor of mammalian collagenase but not of bacterial collagenase. This inhibitor has been partially purified and has an apparent molecular weight of 45,000. It is a glycoprotein and is stable to heat, trypsin, acid and mercurials. Inhibitory activity is destroyed on reductive alkylation. The inhibitor interacts with collagenase and this interaction leads to the loss of enzymatic activity. This inhibitor may play a physiological role in the control of collagen degradation in blood vessels.