McCroskery P A, Wood S, Harris E D
Science. 1973 Oct 5;182(4107):70-1. doi: 10.1126/science.182.4107.70.
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.
一种兔肿瘤胶原酶被纯化了5000多倍。以这种形式，它在37摄氏度、pH值7.6的条件下将螺旋构象的天然胶原降解为两个片段，但它切割明胶的能力很弱，这表明对于这种纯形式的酶来说，底物的高级结构很重要。在体内，除胶原酶外的其他酶可能会降解初级胶原溶解产生的明胶多肽。
