Journal
BIOCHEMISTRY-MOSCOW
Volume 67, Issue 12, Pages 1383-1387Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1023/A:1021814211131
Keywords
Bowman-Birk inhibitor; acylation; unsaturated fatty acids; inhibition constant; trypsin; alpha-chymotrypsin; human leukocyte elastase
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The effect of acylation of Bowman-Birk soybean proteinase inhibitor (BBI) by derivatives of various unsaturated fatty acids on inhibition of trypsin, alpha-chymotrypsin, and human leukocyte elastase was investigated. Inhibition (K-i) and kinetic (k(ass), k(diss)) constants of interaction between proteases and acylated BBI derivatives were determined. For mono-, di-, and triacylated BBI derivatives, insertion of two oleic residues into the BBI molecule was demonstrated to be more potent for exhibiting antiproteinase activity.
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