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

Biochemistry (Moscow) volume 67, pages 1383–1387 (2002)Cite this article

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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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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  • DOI: https://doi.org/10.1023/A:1021814211131

  • Bowman–Birk inhibitor
  • acylation
  • unsaturated fatty acids
  • inhibition constant
  • trypsin
  • α-chymotrypsin
  • human leukocyte elastase