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Study of the interaction of trypsin inhibitor from the sea anemone Radianthus macrodactylus with proteases
Authors:I N Sokotun  O V Gnedenko  A V Leychenko  M M Monastyrnaya  E P Kozlovskaya  A A Molnar  A S Ivanov
Institution:(1) Pacific Institute of Bioorganic Chemistry, Far East Branch of Russian Academy of Sciences, pr. 100 let Vladivostoku 159, Vladivostok, 690022, Russia;(2) Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Pogodinskaya ul., 10, Moscow, 119121, Russia
Abstract: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.
Keywords:sea anemone  protease inhibitor  trypsin  α  -chymotrypsin  dissociation constant  SPR  optical biosensor  Biacore 3000
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