Fragmentation of human polymorphonuclear-leucocyte collagenase.
Fragmentation of human polymorphonuclear-leucocyte collagenase.
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人多形核白细胞胶原酶的断裂。
DOI：
10.1042/bj2910847
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Tschesche,H
中科院分区：
文献类型：
--
作者：
Knäuper,V;Osthues,A;DeClerck,YA;Langley,KE;Bläser,J;Tschesche,H
人多形核白细胞胶原酶(M(R)64,000)显示自身蛋白降解为M(R)40,000和M(R)27,000两个主要片段。N-末端序列数据和底物特异性研究表明，M(R)-40,000片段对应于催化结构域，而M(R0-27,000)片段没有酶活性。M(R)-40,000片段的活性与完整的活性胶原酶(M(R)64,000)的特异性相当，但失去了裂解胶原蛋白的能力。该片段的酶活性可被金属蛋白酶组织抑制因子(TIMP)-1或重组TIMP-2以1：1的摩尔比抑制。该酶的C末端部分(M(R)27000)对与胶原底物的结合反应很重要，参与了胶原酶的降解。
Human polymorphonuclear-leucocyte collagenase (M(r) 64,000) shows autoproteolytic degradation to two major fragments of M(r) 40,000 and M(r) 27,000. N-terminal sequence data and investigation of the substrate specificity of the fragments demonstrate that the M(r)-40,000 fragment corresponds to the catalytic domain, whereas the M(r0-27,000 fragment shows no enzymic activity. The activity profile of the M(r)-40,000 fragment is comparable with the specificity of the intact active collagenase (M(r) 64,000), but the ability to cleave collagen was lost. The enzymic activity of this fragment can be inhibited by either tissue inhibitor of metalloproteinase (TIMP)-1 or recombinant TIMP-2 in a 1:1 molar ratio. The C-terminal part of the enzyme (M(r) 27,000), important for the binding reaction with collagen substrates, is involved in collagenolysis.