Journal Article

Partial Purification and Characterization of a Novel Soybean Protease Which is inhibited by Kunitz and Bowman-Birk Trypsin Inhibitors

Shimpei Morita, Masami Fukase, Kumiko Hoshino, Yoichi Fukuda, Masami Yamaguchi and Yuhei Morita

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 119, issue 4, pages 711-718
Published in print April 1996 | ISSN: 0021-924X
Published online April 1996 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/oxfordjournals.jbchem.a021300
Partial Purification and Characterization of a Novel Soybean Protease Which is inhibited by Kunitz and Bowman-Birk Trypsin Inhibitors

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A novel serine protease has been partially purified from dry seeds of the soybean (Glycine max;) cultivar Keburi by cryoprecipitation at pH 6.4, fractional precipitation with ammonium sulfate, and a series of column chromatographic procedures on DEAE-Sepharose, SP-Sepharose, and Arginine-Sepharose 4B. Some properties of the purified enzyme were studied. The protease hydrolyzed the native storage globulins of soybean seeds, such as the α subunit of β-conglycinin, at a pair of arginine residues, Argl26-Argl27. The proteolysis of the α subunit in the purified α2β molecule of β-conglycinin apparently followed first order kinetics. The enzyme was inhibited by both soybean Kunitz trypsin inhibitor and Bowman-Birk proteinase inhibitor in a competitive manner. Moreover, the enzyme could catalyze the specific proteolysis of the A3 polypeptide of the purified G5 glycinin at the Arg99-Glyl00 linkage, or the carboxyl side of the Arg98-Arg99 paired basic residues.

Keywords: β-conglycinin; glycinin; serine protease; soybean; trypsin inhibitor

Journal Article.  0 words. 

Subjects: Biochemistry

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