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Interaction of Native Bowman-Birk Soybean Protease Inhibitor and Its Hydrophobized Derivative with Multilamellar Vesicles of Soybean Phospholipids

A. S. Balkina1*, A. A. Selischeva2, G. M. Sorokoumova2, and N. I. Larionova1

1Faculty of Chemistry, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (7-495) 939-5417; E-mail: balkina@enzyme.chem.msu.ru

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

* To whom correspondence should be addressed.

Received December 16, 2004; Revision received January 20, 2005
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.
KEY WORDS: protein-lipid complexes, multilamellar vesicles, phospholipids, Bowman-Birk soybean protease inhibitor

DOI: 10.1134/S0006297906010135