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大鼠睾丸中类胶原酶肽酶的金属酶性质

The metalloenzymic nature of collagenase-like peptidase of the rat testis.

作者信息

Lukac J, Koren E

出版信息

J Reprod Fertil. 1977 Jan;49(1):95-9. doi: 10.1530/jrf.0.0490095.

Abstract

Collagenase-like peptidase, an enzyme degrading synthetic collagenase substrate (PZ-pentapeptide), was purified from rat testes and its properties were examined. Its activity was strongly inhibited by chelating agents, such as EDTA and 1,10-phenanthroline. By chelation and exhaustive dialysis it was possible to obtain this enzyme in its inactive, metal-free form. The activity of the metal-free enzyme was partly recovered by treatment with zinc or manganese ions, while a combined zinc and manganese treatment resulted in complete recovery of enzyme activity.

摘要

从大鼠睾丸中纯化出一种类似胶原酶的肽酶,它是一种能降解合成胶原酶底物(PZ-五肽)的酶,并对其性质进行了研究。其活性受到螯合剂(如EDTA和1,10-菲咯啉)的强烈抑制。通过螯合和彻底透析,可以得到无活性的、不含金属的该酶形式。用锌或锰离子处理后,无金属酶的活性部分恢复,而锌和锰联合处理则使酶活性完全恢复。

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