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

   
Sokotun I.N.1, Gnedenko O.V.2, Leychenko E.V.1, Monastyrnaya M.M.1, Kozlovskaya E.P.1, Molnar A.A.2, Ivanov A.S.2

1. Pacific Institute of Bioorganic Chemistry FEB RAS
2. V.N.Orekhovich Institute of Biomedical Chemistry RAMS
Section: Experimental/Clinical Study
PubMed Id: 17288251
Year: 2006  Volume: 52  Issue: 6  Pages: 595-600
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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Keywords: sea anemone, protease inhibitor, trypsin, α-chymotrypsin, dissociation constant, SPR, Biacore 3000
Citation:

Sokotun, I. N., Gnedenko, O. V., Leychenko, E. V., Monastyrnaya, M. M., Kozlovskaya, E. P., Molnar, A. A., Ivanov, A. S. (2006). Interaction investigation of trypsin inhibitor from sea anemone Radianthus macrodactylus with proteases. Biomeditsinskaya Khimiya, 52(6), 595-600.
This paper is also available as the English translation: 10.1134/S1990750807020059
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