Complexing of Basic Pancreatic Proteinase Inhibitor with Soybean Phospholipid Multilamellar Vesicles

O. P. Tiourina¹, T. V. Sharf², A. A. Selishcheva¹, G. M. Sorokoumova², V. I. Shvets², and N. I. Larionova^1*

¹School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-5417; E-mail: nilar@enzyme.chem.msu.ru

²Lomonosov Moscow State Academy of Fine Chemical Technology, pr. Vernadskogo 84, Moscow, 117571 Russia; fax: (095) 434-8233; E-mail: biotechnology@mtu-net.ru

^* To whom correspondence should be addressed.

Received July 10, 2000; Revision received December 15, 2000

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The formation of complexes of basic pancreatic proteinase inhibitor (BPTI) with multilamellar vesicles (MLV) from six preparations of soybean phospholipids of various composition was studied. When BPTI, a non-membrane protein, interacts with MLV, the vesicles aggregate, forming a precipitate of protein-lipid complexes. The BPTI content in the protein-lipid complexes increases with decreasing pH of the medium and on addition of negatively charged components into the lipid mixture. The protein-induced aggregation of the phospholipid vesicles is suggested to be mainly determined by electrostatic forces. The antiproteinase activity of BPTI in the complexes was rather low but increased up to 70% of the initial activity on addition of an ionic detergent (sodium deoxycholate).

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KEY WORDS: protein-lipid interaction, multilamellar phospholipid vesicles, BPTI, inhibiting activity

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