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Study of Antiproteinase Activity of Acylated Derivatives of Bowman–Birk Soybean Proteinase Inhibitor

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Abstract

The effect of acylation of Bowman–Birk soybean proteinase inhibitor (BBI) by derivatives of various unsaturated fatty acids on inhibition of trypsin, α-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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Authors and Affiliations

  1. Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119992, Russia

    E. V. Malykh & N. I. Larionova

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  1. E. V. Malykh
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  2. N. I. Larionova
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Correspondence to N. I. Larionova.

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Malykh, E.V., Larionova, N.I. Study of Antiproteinase Activity of Acylated Derivatives of Bowman–Birk Soybean Proteinase Inhibitor. Biochemistry (Moscow) 67, 1383–1387 (2002). https://doi.org/10.1023/A:1021814211131

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