Studies on soybean trypsin inhibitors. XIII. Preparation and characterization of active fragments from Bowman-Birk proteinase inhibitor.

Abstract:

:Soybean Bowman-Birk inhibitor, a double-headed inhibitor of trypsin and alpha-chymotrypsin, was treated with cyanogen bromide and then pepsin to yield two inhibitory active fragments. Structural investigation showed that one of the fragments was derived from the trypsin inhibitory domain and the other from the chymotrypsin inhibitory domain of the inhibitor. In contrast to the unusual stability of the native inhibitor, the separated domains were less stable and could be inactivated with excess proteinases. These results suggest that the legume double-headed inhibitors acquired their unusual stability by duplicating an ancestral single-headed structure.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Odani S,Ikenaka T

doi

10.1093/oxfordjournals.jbchem.a131968

subject

Has Abstract

pub_date

1978-03-01 00:00:00

pages

747-53

issue

3

eissn

0021-924X

issn

1756-2651

journal_volume

83

pub_type

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