title: [Interaction investigation of trypsin inhibitor from sea anemone Radianthus macrodactylus with proteases].
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, alpha-chymotrypsin, plasmin, thrombin, kallikrein), cysteine protease (papain) and aspartic protease (pepsin). Inhibitor VJ interacted only with trypsin and 6-chymotrypsin. Kinetic and thermodynamics parameters of intermolecular complexes formation were determined: KD = 7,38 x 10(-8) M and 9,93 x 10(-7) M for pairs InhVJ/trypsin and InhVJ/alpha-chymotrypsin, respectively.
authors.forename: I N
authors.initials: IN
authors.lastname: Sokotun
authors.forename: O V
authors.initials: OV
authors.lastname: Gnedenko
authors.forename: E V
authors.initials: EV
authors.lastname: Leĭchenko
authors.forename: M M
authors.initials: MM
authors.lastname: Monastyrnaia
authors.forename: E P
authors.initials: EP
authors.lastname: Kozlovskaia
authors.forename: A A
authors.initials: AA
authors.lastname: Mol'nar
authors.forename: A C
authors.initials: AC
authors.lastname: Ivanov
mesh_terms: D000818:Animals; D006801:Humans; D007700:Kinetics; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D012615:Sea Anemones / Q000737:chemistry* / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D014361:Trypsin Inhibitors; D010447:Peptide Hydrolases