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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Original Russian Text © I.N. Sokotun, O.V. Gnedenko, A.V. Leychenko, M.M. Monastyrnaya, E.P. Kozlovskaya, A.A. Molnar, A.S. Ivanov, 2007, published in Biomeditsinskaya Khimiya.
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Sokotun, I.N., Gnedenko, O.V., Leychenko, A.V. et al. Study of the interaction of trypsin inhibitor from the sea anemone Radianthus macrodactylus with proteases. Biochem. Moscow Suppl. Ser. B 1, 139–142 (2007). https://doi.org/10.1134/S1990750807020059
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DOI: https://doi.org/10.1134/S1990750807020059