Cawston T E, Mercer E
FEBS Lett. 1986 Dec 1;209(1):9-12. doi: 10.1016/0014-5793(86)81074-2.
The binding of collagenase to both alpha 2-macroglobulin and the tissue inhibitor of metalloproteinases was studied using purified materials. Collagenase bound preferentially to alpha 2-macroglobulin although no transfer of collagenase to alpha 2-macroglobulin occurred if the enzyme was first mixed with the tissue inhibitor of metalloproteinases. The sequences of amino acids in both inhibitors likely to be responsible for the binding of collagenase are discussed and compared to the cleavage site in the collagen molecule.
使用纯化的材料研究了胶原酶与α2-巨球蛋白和金属蛋白酶组织抑制剂的结合情况。胶原酶优先与α2-巨球蛋白结合，不过，如果该酶首先与金属蛋白酶组织抑制剂混合，则不会发生胶原酶向α2-巨球蛋白的转移。讨论了两种抑制剂中可能负责胶原酶结合的氨基酸序列，并将其与胶原分子中的切割位点进行了比较。
