Interaction investigation of trypsin inhibitor from sea anemone radianthus macrodactylus with proteases

   


1. Pacific Institute of Bioorganic Chemistry FEB RAS
2. V.N.Orekhovich Institute of Biomedical Chemistry RAMS
Type: Experimental/clinical study
PubMed Id: 17288251
Year: 2006 vol: 52  issue:6  pages: 595-600
Abstract: The interaction of inhibitor VJ (InhVJ), isolated from sea anemone R. macrodactylus, with different proteases was investigated. The following enzymes were tested: serine proteases (trypsin, α−chymotrypsin, plasmin, thrombin, kallikrein), cysteinе protease (papain) and aspartic protease (pepsin). Inhibitor VJ interacted only with trypsin and б-chymotrypsin. Kinetic and thermodynamics parameters of intermolecular complexes formation were determined: KD=7,3810-8 М and 9,9310-7 М for pairs InhVJ/trypsin and InhVJ/α-chymotrypsin, respectively.
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Reference: Sokotun I.N., Gnedenko O.V., Leychenko Е.V., Monastyrnaya М.М., Kozlovskaya E.P., Molnar A.A., Ivanov A.S., Interaction investigation of trypsin inhibitor from sea anemone radianthus macrodactylus with proteases, Biomeditsinskaya khimiya, 2006, vol: 52(6), 595-600.
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