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

Autor:	I N, Sokotun, O V, Gnedenko, E V, Leĭchenko, M M, Monastyrnaia, E P, Kozlovskaia, A A, Mol'nar, A C, Ivanov
Rok vydání:	2007
Předmět:	Kinetics Sea Anemones Animals Humans Trypsin Inhibitors Peptide Hydrolases Protein Binding
Zdroj:	Biomeditsinskaia khimiia. 52(6)
ISSN:	2310-6972
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::61133c468d4678429530a9261e009013 https://pubmed.ncbi.nlm.nih.gov/17288251 Zobrazit plný text záznamu