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Participation of 650-kDa protease (20 S proteasome) in starfish oocyte maturation.

作者信息

Sawada M T, Someno T, Hoshi M, Sawada H

机构信息

Department of Life Science, Faculty of Science, Tokyo Institute of Technology, Japan.

出版信息

Dev Biol. 1992 Apr;150(2):414-8. doi: 10.1016/0012-1606(92)90252-c.

DOI:10.1016/0012-1606(92)90252-c
PMID:1551483
Abstract

A protease involved in oocyte maturation of a starfish, Asterina pectinifera, was explored. Trypsin-like and chymotrypsin-like activities of the 650-kDa protease in oocyte extract were revealed to increase more than twice under the influence of 1-methyladenine before germinal vesicle breakdown (GVBD) during maturation. The inhibitory potencies of leupeptin and its five analogs against the chymotrypsin-like activity, but not the trypsin-like activity, of this protease was well in accord with those against GVBD (Takagi Sawada et al. (1989). Dev. Biol. 133, 609-612). These results indicate that the chymotrypsin-like activity of the 650-kDa protease (most probably 20 S proteasome) plays a key role in starfish oocyte maturation.

摘要

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海星的卵母细胞成熟是由一种G蛋白的βγ亚基复合物介导的。
J Cell Biol. 1993 May;121(4):775-83. doi: 10.1083/jcb.121.4.775.
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An Arabidopsis gene homologous to mammalian and insect genes encoding the largest proteasome subunit.一个与编码最大蛋白酶体亚基的哺乳动物和昆虫基因同源的拟南芥基因。
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