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Interaction of native Bowman—Birk soybean protease inhibitor and its hydrophobized derivative with multilamellar vesicles of soybean phospholipids

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Abstract

The interaction of native Bowman-Birk soybean protease inhibitor (BBI) and its hydrophobized derivative with multilamellar vesicles of various soybean phospholipids was investigated. Decrease in pH and introduction of negatively charged components to the lipid mixture increased BBI content in the protein-lipid complex. This suggests a contribution of electrostatic forces in the protein-lipid interaction. Protein hydrophobization insignificantly influenced BBI binding to lipids. In the complex with lipids, both proteins (BBI and its hydrophobized derivative) retained high anti-chymotrypsin activity (75–100%), which was not influenced by the presence of the ionic detergent sodium deoxycholate.

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Abbreviations

BBI:

Bowman-Birk soybean protease inhibitory

BPTI:

basic pancreatic trypsin inhibitor

DOC:

sodium deoxycholate

LP:

soybean lipid preparation

MLV:

multilamellar vesicles

PC:

phosphatidylcholine

PE:

phosphatidylethanolamine

PG:

phosphatidylglycerol

PI:

phosphatidylinositol

lyso-PC:

lysophosphatidylcholine

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Authors and Affiliations

  1. Faculty of Chemistry, Lomonosov Moscow State University, 119992, Moscow, Russia

    A. S. Balkina & N. I. Larionova

  2. Lomonosov Academy of Fine Chemical Technology, pr. Vernadskogo 84, 117571, Moscow, Russia

    A. A. Selischeva & G. M. Sorokoumova

Authors
  1. A. S. Balkina
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  2. A. A. Selischeva
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  3. G. M. Sorokoumova
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  4. N. I. Larionova
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Additional information

Original Russian Text © A. S. Balkina, A. A. Selischeva, G. M. Sorokoumova, N. I. Larionova, 2006, published in Biokhimiya, 2006, Vol. 71, No. 1, pp. 103–110.

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Balkina, A.S., Selischeva, A.A., Sorokoumova, G.M. et al. Interaction of native Bowman—Birk soybean protease inhibitor and its hydrophobized derivative with multilamellar vesicles of soybean phospholipids. Biochemistry (Moscow) 71, 84–89 (2006). https://doi.org/10.1134/S0006297906010135

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  • DOI: https://doi.org/10.1134/S0006297906010135

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