Balkina A S, Selischeva A A, Sorokoumova G M, Larionova N I
Faculty of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
Biochemistry (Mosc). 2006 Jan;71(1):84-9. doi: 10.1134/s0006297906010135.
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.
研究了天然的鲍曼-伯克大豆蛋白酶抑制剂（BBI）及其疏水化衍生物与各种大豆磷脂多层囊泡的相互作用。降低pH值并向脂质混合物中引入带负电荷的成分会增加蛋白质-脂质复合物中的BBI含量。这表明静电力在蛋白质-脂质相互作用中起作用。蛋白质疏水化对BBI与脂质的结合影响不大。在与脂质形成的复合物中，两种蛋白质（BBI及其疏水化衍生物）均保留了较高的抗胰凝乳蛋白酶活性（75-100%），该活性不受离子去污剂脱氧胆酸钠存在的影响。
