标题:Bombyx acid cysteine proteinase
作者:Takahashi, SY; Yamamoto, Y; Zhao, XF; Watabe, S
通讯作者:Takahashi, SY
作者机构:[Takahashi, SY; Yamamoto, Y; Zhao, XF; Watabe, S]SHANDONG UNIV,DEPT BIOL,SHANDONG,PEOPLES R CHINA.;[Takahashi, SY; Yamamoto, Y; Zhao, XF; 更多
会议名称:7th International Congress on Invertebrate Reproduction
会议日期:AUG 05-11, 1995
来源:INVERTEBRATE REPRODUCTION & DEVELOPMENT
出版年:1996
卷:30
期:1-3
页码:265-281
DOI:10.1080/07924259.1996.9672553
关键词:BCP; pro-cysteine proteinase; yolk protein degradation
摘要:Three kinds of yolk proteins (vitellin, egg-specific protein and 30 k-proteins) are found in silkmoth eggs and have been well characterized. Essentially these proteins are considered to be amino acid reserves for developing embryos. Since at an early stage of egg development the cysteine proteinase accounts for the majority of the total proteinase activity, it may be involved in the degradation of yolk proteins. The enzyme is stored in the eggs as an inactive pro-form, indicating that the activation of the enzyme might be one of the key steps in yolk protein degradation. To investigate at the molecular level how yolk proteins degradation takes place, we have studied Bombyx acid cysteine proteinase (BCP) during an early period of embryonic development. We summarize how proteinases are regulated and are involved in the degradation of Bombyx yolk proteins during embryogenesis. These will be discussed mainly in light of recent results obtained from eggs of the silkmoth, Bombyx mori.
收录类别:CPCI-S;SCOPUS;SCIE
WOS核心被引频次:22
Scopus被引频次:21
资源类型:会议论文;期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030433850&doi=10.1080%2f07924259.1996.9672553&partnerID=40&md5=94370625b13632e08ce9d4e32fea1d6f
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