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镧系元素对人类风湿性滑膜分泌的中性蛋白酶的抑制作用。

Inhibition, by lanthanides, of neutral proteinases secreted by human, rheumatoid synovium.

作者信息

Evans C H, Ridella J D

出版信息

Eur J Biochem. 1985 Aug 15;151(1):29-32. doi: 10.1111/j.1432-1033.1985.tb09064.x.

DOI:10.1111/j.1432-1033.1985.tb09064.x
PMID:2992958
Abstract

Fragments of human, rheumatoid synovium were maintained on organ culture for three days under serum-less conditions. Their conditioned media contained collagenolytic, gelatinolytic and caseinolytic activities, which were susceptible to inhibition by lanthanide ions. Of the four lanthanides tested, Sm3+ proved the best inhibitor of gelatinase and caseinase, while La3+ inhibited collagenase the most strongly. Inhibition of collagenase by La3+ was uncompetitive. A direct binding assay confirmed the greater association between collagen fibrils and collagenase in the presence of La3+. Ca2+ was not required for binding of the uninhibited enzyme to collagen, but acted to stabilize collagenase against thermoinactivation.

摘要

人类风湿性滑膜碎片在无血清条件下进行器官培养三天。其条件培养基含有胶原分解活性、明胶分解活性和酪蛋白分解活性,这些活性易受镧系离子抑制。在所测试的四种镧系元素中,Sm3+被证明是明胶酶和酪蛋白酶的最佳抑制剂,而La3+对胶原酶的抑制作用最强。La3+对胶原酶的抑制是非竞争性的。直接结合试验证实,在La3+存在的情况下,胶原纤维与胶原酶之间的结合更强。未受抑制的酶与胶原的结合不需要Ca2+,但Ca2+可使胶原酶稳定,防止热失活。

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1
Inhibition, by lanthanides, of neutral proteinases secreted by human, rheumatoid synovium.镧系元素对人类风湿性滑膜分泌的中性蛋白酶的抑制作用。
Eur J Biochem. 1985 Aug 15;151(1):29-32. doi: 10.1111/j.1432-1033.1985.tb09064.x.
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The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor.金属蛋白酶组织抑制剂(TIMP-2)与72 kDa前明胶酶之间的复合物是一种金属蛋白酶抑制剂。
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