Study of antiproteinase activity of acylated derivatives of Bowman-Birk soybean proteinase inhibitor |
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Authors: | Malykh E V Larionova N I |
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Affiliation: | (1) Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119992, Russia |
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Abstract: | The effect of acylation of Bowman–Birk soybean proteinase inhibitor (BBI) by derivatives of various unsaturated fatty acids on inhibition of trypsin, -chymotrypsin, and human leukocyte elastase was investigated. Inhibition (Ki) and kinetic (kass, kdiss) 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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Keywords: | Bowman– Birk inhibitor acylation unsaturated fatty acids inhibition constant trypsin /content/w6t48004325n4373/xxlarge945.gif" alt=" agr" align=" BASELINE" BORDER=" 0" >-chymotrypsin human leukocyte elastase |
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