Study of the interaction of trypsin inhibitor from the sea anemone Radianthus macrodactylus with proteases |
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Authors: | I N Sokotun O V Gnedenko A V Leychenko M M Monastyrnaya E P Kozlovskaya A A Molnar A S Ivanov |
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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 |
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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. |
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Keywords: | sea anemone protease inhibitor trypsin α -chymotrypsin dissociation constant SPR optical biosensor Biacore 3000 |
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