金属蛋白酶组织抑制剂（TIMP）从酶复合物中解离后会产生完全有活性的抑制剂。
Dissociation of tissue inhibitor of metalloproteinases (TIMP) from enzyme complexes yields fully active inhibitor.
作者信息
Murphy G, Koklitis P, Carne A F
机构信息
Strangeways Research Laboratory, Cambridge, U.K.
出版信息
Biochem J. 1989 Aug 1;261(3):1031-4. doi: 10.1042/bj2611031.
Recombinant human tissue inhibitor of metalloproteinases (TIMP) forms complexes with high-Mr active recombinant stromelysin that are stable over long periods under physiological conditions. TIMP-stromelysin complexes could be dissociated in the presence of EDTA at pH 3, releasing free TIMP and destroying stromelysin activity. The dissociated TIMP was apparently unmodified, in contrast with other known protein inhibitors of metalloproteinases and many classes of serine-proteinase inhibitor, which are slowly cleaved.
重组人金属蛋白酶组织抑制剂（TIMP）与高Mr活性重组基质溶解素形成复合物，该复合物在生理条件下能长期稳定存在。TIMP-基质溶解素复合物在pH 3的EDTA存在下可解离，释放出游离的TIMP并破坏基质溶解素的活性。与其他已知的金属蛋白酶蛋白抑制剂和许多类丝氨酸蛋白酶抑制剂不同，解离后的TIMP显然未被修饰，后两者会被缓慢裂解。
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