Gelatin: a poor substrate for a mammalian collegenase

A rabbit tumor collagenase was purified more than 5000-fold. In this form it degrades native collagen in helical conformation at 37 degrees C, pH 7.6, into two fragments, but it had little capacity to cleave gelatin, an indication of the importance of higher-order structure of substrate for this enzyme in pure form. It is likely that, in vivo, enzymes other than collagenase degrade gelatin polypeptides produced by primary collagenolysis.