Huang C C, Wu C H, Abramson M
Biochim Biophys Acta. 1979 Sep 12;570(1):149-56. doi: 10.1016/0005-2744(79)90209-2.
A specific collagenase (EC 3.4.24.3) has been found and purified from serum-free culture medium of 11095 epidermoid carcinoma of rat prostate. The molecular weight of this collagenase was estimated at 71 000 and the pH optimum was approx. 7. At 26 degrees C, the collagenase cleaved collagen at a site 3/4 the length from the N-terminus. At 37 degrees C, this collagenase degraded collagen to smaller peptides. The enzyme activity was inhibited by serum, cysteine and EDTA, but not by protease inhibitors. The presence of collagenase in rat tumor tissue suggests that this enzyme might play a significant role in tissue invasion by cancer cells.
已从大鼠前列腺11095表皮样癌的无血清培养基中发现并纯化出一种特定的胶原酶(EC 3.4.24.3)。这种胶原酶的分子量估计为71000,最适pH约为7。在26℃时,该胶原酶在距N端3/4长度处切割胶原蛋白。在37℃时,这种胶原酶将胶原蛋白降解为较小的肽段。该酶的活性受到血清、半胱氨酸和EDTA的抑制,但不受蛋白酶抑制剂的抑制。大鼠肿瘤组织中存在胶原酶表明该酶可能在癌细胞的组织侵袭中发挥重要作用。