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大豆萌发和幼苗生长过程中β-伴大豆球蛋白降解产生的30 kDa片段的特性分析

Characterization of 30-kDa fragments derived from beta-conglycinin degradation process during germination and seedling growth of soybean.

作者信息

Kawai M, Suzuki S, Asano M, Miwa T, Shibai H

机构信息

Food Research & Development Laboratories, Ajinomoto Co., Inc., Japan.

出版信息

Biosci Biotechnol Biochem. 1997 May;61(5):794-9. doi: 10.1271/bbb.61.794.

Abstract

The degradation process of beta-conglycinin, a vicilin-type glycosylated storage protein of soybean seeds, during germination and seedling growth was examined by concanavalin A blotting combined with polyacrylamide gel electrophoresis. We detected and analyzed the structures of key intermediary fragments of 30 kDa derived from beta-conglycinin degradation, they were proved to be single-domain type subunits of beta-conglycinin. We show here a degradation process of beta-conglycinin: beta-conglycinin is subjected to limited proteolysis at exposed regions on the molecular surface, like domain junctions, generating 30-kDa single-domain fragments before non-specific proteolysis.

摘要

通过伴刀豆球蛋白A印迹结合聚丙烯酰胺凝胶电泳,研究了大豆种子中的一种豌豆球蛋白型糖基化贮藏蛋白β-伴大豆球蛋白在萌发和幼苗生长过程中的降解过程。我们检测并分析了β-伴大豆球蛋白降解产生的30 kDa关键中间片段的结构,它们被证明是β-伴大豆球蛋白的单结构域型亚基。我们在此展示了β-伴大豆球蛋白的降解过程:β-伴大豆球蛋白在分子表面的暴露区域(如结构域连接处)受到有限的蛋白水解作用,在非特异性蛋白水解之前产生30 kDa的单结构域片段。

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