Synergistic interaction of a protease and protease inhibitors from Russell's viper (Vipera russelli) venom.
An acidic proteolytic enzyme, RVVX, was purified from Vipera russelli venom by successive chromatography on CM-Sephadex C-25, DEAE-cellulose and Sephadex G-100 columns. RVVX is a glycoprotein with a mol. wt of 79,000. It exhibited caseinolytic and factor X activating properties. Two trypsin inhibitors, TI-I and TI-II, were purified from V. russelli venom in a single step by CM-Sephadex C-25 column chromatography. The trypsin inhibitors interacted with the proteolytic enzyme RVVX. TI-I inhibited only the factor X activating property of RVVX while TI-II inhibited both, the caseinolytic and also factor X activating properties of RVVX. The edema inducing activity of RVVX increased markedly in the presence of non-edema inducing doses of TI-I and TI-II. RVVX, TI-I and TI-II were non-lethal in mice. The combination of RVVX and TI-II demonstrated enhanced toxicity.
Department of Biochemistry, University of Mysore, Manasagangotri, India.
G P
GP
Jayanthi
T V
TV
Gowda
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004357:Drug Synergism; D004487:Edema / Q000139:chemically induced; D004591:Electrophoresis, Polyacrylamide Gel; D005170:Factor X / Q000378:metabolism; D007928:Lethal Dose 50; D051379:Mice; D010447:Peptide Hydrolases / Q000032:analysis / Q000302:isolation & purification / Q000633:toxicity*; D011480:Protease Inhibitors / Q000032:analysis / Q000302:isolation & purification / Q000633:toxicity*; D013050:Spectrometry, Fluorescence; D014361:Trypsin Inhibitors / Q000302:isolation & purification; D014757:Viper Venoms / Q000032:analysis / Q000633:toxicity*
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D014757:Viper Venoms; D005170:Factor X; D010447:Peptide Hydrolases