THE INTERACTION OF PURIFIED RABBIT BONE COLLAGENASE WITH PURIFIED RABBIT BONE METALLOPROTEINASE INHIBITOR
THE INTERACTION OF PURIFIED RABBIT BONE COLLAGENASE WITH PURIFIED RABBIT BONE METALLOPROTEINASE INHIBITOR
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DOI：
10.1042/bj2110313
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发表时间：
1983-01-01
影响因子：
4.1
通讯作者：
REYNOLDS, JJ
中科院分区：
文献类型：
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作者：
CAWSTON, TE;MURPHY, G;REYNOLDS, JJ
纯兔骨金属蛋白酶抑制剂(TIMP)与纯兔骨胶原酶结合紧密，表观解离常数Kd为1.4倍。10-10M的酶-抑制物复合体的相对分子质量为54000，但经汞或蛋白酶处理后，该复合体中的酶活性不能恢复。因此，该复合体在大小、对汞的敏感性和在刀豆蛋白A-琼脂糖凝胶上的行为方面不同于潜伏胶原酶。比较了纯化组分与粗胶原酶和粗酶抑制剂在培养基中的相互作用。汞处理部分逆转了粗体系中的抑制作用，但在使用纯化成分时不能。结果的意义被讨论与细胞外控制胶原酶的活性有关。
Pure rabbit bone metalloproteinase inhibitor (TIMP) bound tightly to pure rabbit bone collagenase with an apparent Kd of 1.4 .times. 10-10 M. MW of the enzyme-inhibitor complex was 54,000 but no enzyme activity could be recovered from the complex after treatment with mercurials or proteinases. The complex thus differed from latent collagenase in terms of size, susceptibility to mercurials and behavior on concanavalin A-Sepharose. Interaction of the purified components was compared with that of crude collagenase and crude inhibitor in culture medium. Mercurial treatment partially reversed the inhibition in the crude system but not when the purified components were used. Significance of the results is discussed in relation to the extracellular control of the activity of collagenase.