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兔植入前子宫液中一种类胰蛋白酶的部分纯化及特性分析

Partial purification and characterization of a trypsin-like proteinase from rabbit preimplantation uterine fluid.

作者信息

Tisljar U, Denker H W

出版信息

Biol Chem Hoppe Seyler. 1985 Nov;366(11):1053-5. doi: 10.1515/bchm3.1985.366.2.1053.

DOI:10.1515/bchm3.1985.366.2.1053
PMID:3907661
Abstract

Previous investigations have proved that proteinases are involved in implantation of the rabbit embryo into the uterine tissues. This study describes a trypsin-like enzyme found in the blastocyst fluid and uterine flushings at the time of implantation. The proteinase isolated from uterine flushings has a molecular mass of about 50 kDa and exists in two differently charged forms of pI 4.0 and 4.5. Tests with low molecular mass 4-nitroanilide substrates proved a marked cleavage selectivity of the enzyme for arginyl bonds. The catalytic activity is not affected by Ca2+ and EDTA but inhibited by aprotinin and a high concentration (10(-6)M) of lima bean trypsin inhibitor.

摘要

先前的研究已证明蛋白酶参与兔胚胎植入子宫组织的过程。本研究描述了在植入时囊胚液和子宫冲洗液中发现的一种类胰蛋白酶。从子宫冲洗液中分离出的蛋白酶分子量约为50 kDa,以两种不同电荷形式存在,其等电点分别为4.0和4.5。用低分子量4-硝基苯胺底物进行的测试证明该酶对精氨酰键具有显著的切割选择性。其催化活性不受Ca2+和EDTA的影响,但受抑肽酶和高浓度(10(-6)M)的 lima 豆胰蛋白酶抑制剂抑制。

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