PMID: 3886572Feb 1, 1985Paper

The Bowman-Birk inhibitor. Trypsin- and chymotrypsin-inhibitor from soybeans

International Journal of Peptide and Protein Research
Y Birk

Abstract

Four decades of studies on the isolation, characterization, properties, structure, function and possible uses of the Bowman-Birk trypsin- and chymotrypsin-inhibitor from soybeans are reviewed. Starting from Bowman's Acetone Insoluble factor, designated Ai, AA and SBTIAA, the Bowman-Birk inhibitor (BBI) was found to be a protein molecule consisting of a chain of 71 amino acids cross linked by 7 disulfide bonds, with a tendency to self-associate. BBI possesses two independent sites of inhibition, one at Lys 16-Ser 17 against trypsin and the other at Leu 43-Ser 44 against chymotrypsin. It forms a 1:1 complex with either trypsin or chymotrypsin and a ternary complex with both enzymes. Ingestion of BBI by rats, chicks or quails affects the size and protein biosynthesis of the pancreas. Establishment of the full covalent structure of BBI revealed a high homology in the sequences around the two inhibitory sites, suggesting evolutionary gene duplication from a single-headed ancestral inhibitor. Scission of BBI by CNBr followed by pepsin results in two active fragments, one that inhibits trypsin and the other, chymotrypsin. Replacements and substitutions in the reactive sites result in changes in inhibitory activity and in specificity o...Continue Reading

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Related Concepts

Acetone
Avazyme
Enzyme Inhibitors
Biological Evolution
Photochemistry
Protein Conformation
Glycine max
Structure-Activity Relationship
Trypsin Inhibitor, Bowman-Birk Soybean
Trypsin Inhibitors

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