GLYCININ-A4A5 SUBUNIT DIGESTING PROTEASE IN SOYBEAN SEEDS

被引：7

作者：

AKHTARUZZAMAN, M ^{[1
]}

KIMURA, Y ^{[1
]}

TAKAGI, S ^{[1
]}

机构：

[1] OKAYAMA UNIV, GRAD SCH NAT SCI & TECHNOL, DIV BIORESOURCE SCI, OKAYAMA 700, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1992年 / 56卷 / 06期

关键词：

D O I：

10.1271/bbb.56.878

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Endopeptidase was partially purified from the globulin fraction of 4-hr-imbibed soybean seeds. The protease fraction obtained had proteolytic activity on the glycinin A4A5 subunit at both pH 4 and 8. A suitable peptidic substrate for the endopeptidase was isolated from the tryptic digest of the carboxymethylated A4A5 subunit. Using the tryptic peptide of glycinin A5 subunit, a simple assay system for the soybean endopeptidase activity has been established. The activity was significantly inhibited by phenylmethylsulfonyl fluoride, indicating the endopeptidase is a serine protease.

引用

页码：878 / 883

页数：6

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