Studies on soybean trypsin inhibitors. X. Isolation and partial characterization of four soybean double-headed proteinase inhibitors.

Abstract:

:Four Bowman-Birk type double-headed inhibitors (B, C-II, D-II, and E-I) were isolated from soybeans. Inhibitor B was different from Bowman-Birk inhibitor only in chromatographic behavior. One mole of C-II inhibited one mole each of bovine trypsin and bovine alpha-chymotrypsin, probably at the same site, and porcine elastase at another reactive site. In the ordinary assay system D-II and E-I inhibited only trypsin activity at a non-stoichiometric inhibitor-enzyme ratio of 1:1.4, and the complexes had rather high dissociation constants. These inhibitors were all inactive toward subtilisin BPN'.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Odani S,Ikenaka T

doi

10.1093/oxfordjournals.jbchem.a131845

subject

Has Abstract

pub_date

1977-12-01 00:00:00

pages

1513-22

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

82

pub_type

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