[Interaction investigation of trypsin inhibitor from sea anemone Radianthus macrodactylus with proteases].
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.
Sokotun
I N
IN
Gnedenko
O V
OV
Leĭchenko
E V
EV
Monastyrnaia
M M
MM
Kozlovskaia
E P
EP
Mol'nar
A A
AA
Ivanov
A C
AC
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
D014361:Trypsin Inhibitors; D010447:Peptide Hydrolases