Merkel J R, Dreisbach J H
Biochemistry. 1978 Jul 11;17(14):2857-63. doi: 10.1021/bi00607a025.
A true collagenase was isolated from the culture fluid of a marine bacterium which has been designated Vibrio B-30 (ATCC 21250). Collagenase production was obtained only in media containing collagen or certain degradation products of collagen. Partial purification on DEAE-cellulose and Sephadex G-200 columns produced active enzyme which was free of nonspecific proteases but which contained two collagenases. The two collagenases have the same apparent molecular size, and evidence is presented to support the theory that one collagenase is derived from the other. Vibrio B-30 collagenase appears to be a tetramer with a molecular weight of about 105 000 composed of two different subunits (mol wt 24 000 and 28 000). Some of the properties of the Vibrio collagenase are compared with those of Clostridium histolyticum collagenase. Molecular weights, subunit structures, specificity and mode of collagen hydrolysis, insensitivity to diisopropyl fluorophosphate and calf serum, and sensitivity to certain metal ion complexing agents and isopropyl alcohol are similar for the collagenases from both organisms. However, Vibrio B-30 collagenase and Clostridium collagenase differ immunologically and electrophoretically.
从一种海洋细菌的培养液中分离出一种真正的胶原酶，该细菌被命名为弧菌B - 30（美国典型培养物保藏中心21250号）。仅在含有胶原蛋白或某些胶原蛋白降解产物的培养基中才能产生胶原酶。在DEAE - 纤维素和葡聚糖G - 200柱上进行部分纯化后，得到了活性酶，该酶不含非特异性蛋白酶，但含有两种胶原酶。这两种胶原酶具有相同的表观分子大小，并且有证据支持一种胶原酶由另一种胶原酶衍生而来的理论。弧菌B - 30胶原酶似乎是一种四聚体，分子量约为105000，由两种不同的亚基（分子量分别为24000和28000）组成。将弧菌胶原酶的一些特性与溶组织梭菌胶原酶的特性进行了比较。两种生物体的胶原酶在分子量、亚基结构、胶原蛋白水解的特异性和方式、对二异丙基氟磷酸酯和小牛血清的不敏感性以及对某些金属离子络合剂和异丙醇的敏感性方面相似。然而，弧菌B - 30胶原酶和梭菌胶原酶在免疫学和电泳方面存在差异。
