Study of the interaction of trypsin inhibitor from the sea anemone Radianthus macrodactylus with proteases

被引：0
作者：
I. N. Sokotun
O. V. Gnedenko
A. V. Leychenko
M. M. Monastyrnaya
E. P. Kozlovskaya
A. A. Molnar
A. S. Ivanov
机构：
[1] Far East Branch of Russian Academy of Sciences,Pacific Institute of Bioorganic Chemistry
[2] Russian Academy of Medical Sciences,Orekhovich Institute of Biomedical Chemistry
来源：
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry | 2007年 / 1卷 / 2期
关键词：
sea anemone; protease inhibitor; trypsin; α-chymotrypsin; dissociation constant; SPR; optical biosensor; Biacore 3000;
D O I：
10.1134/S1990750807020059
中图分类号：
学科分类号：
摘要：
The interaction of the inhibitor VJ (InhVJ), isolated from sea anemone R. macrodactylus, with different proteases was investigated using the method of biosensor analysis. The following enzymes were tested: serine proteases (trypsin, α-chymotrypsin, plasmin, thrombin, kallikrein), cysteina protease (papain) and aspartic protease (pepsin). In the rage of the concentrations studied (10–400 nM) inhibitor VJ interacted only with trypsin and α-chymotrypsin. The intermolecular complexes formation between inhibitor VJ and each of these enzymes was characterized by the following kinetic and thermodynamics parameters: KD = 7.38 × 10−8 M and 9.93 × 10−7 M for pairs InhVJ/trypsin and InhVJ/α-chymotrypsin, respectively.
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页码：139 / 142
页数：3
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