Murphy G, Cawston T E, Galloway W A, Barnes M J, Bunning R A, Mercer E, Reynolds J J, Burgeson R E
Biochem J. 1981 Dec 1;199(3):807-11. doi: 10.1042/bj1990807.
Gel-filtration chromatography of culture medium from rabbit bone explants separates three latent metalloproteinases with activities against collagen, proteoglycan and gelatin respectively. The fractions degrading proteoglycan also degrade laminin, fibronectin and the polymeric products of pepsin-solubilized type IV collagen and can also solubilize insoluble type IV collagen. The fractions degrading gelatin are capable of degrading solubilized type V and 1 alpha,2 alpha,3 alpha (cartilage) collagens, as well as the lower-molecular-weight products of pepsin-solubilized type IV collagen. All activities can be inhibited by 1,10-phenanthroline and occur in either partially or totally latent forms that can be activated by 4-aminophenylmercuric acetate.
对兔骨外植体培养基进行凝胶过滤层析，分离出三种潜在的金属蛋白酶，它们分别对胶原蛋白、蛋白聚糖和明胶具有活性。降解蛋白聚糖的组分还能降解层粘连蛋白、纤连蛋白以及胃蛋白酶溶解的IV型胶原蛋白的聚合产物，并且还能溶解不溶性IV型胶原蛋白。降解明胶的组分能够降解溶解的V型和1α、2α、3α（软骨）胶原蛋白，以及胃蛋白酶溶解的IV型胶原蛋白的低分子量产物。所有活性都能被1,10 - 菲咯啉抑制，并且以部分或完全潜在的形式存在，可被乙酸4 - 氨基苯汞激活。
