The binding of snake venom cardiotoxins to heart cell membranes.
Cobra venom cardiotoxins have the effect, inter alia, of causing systolic arrest of the heart. We have observed significant binding in vitro of 35S-labelled cardiotoxins to mouse heart cell membranes. Part of the binding was saturable and could be displaced with homologous unlabelled cardiotoxins but not by neurotoxins or cardiotoxins inactivated by chemical modification. The specifically bound component represented more than 70% of total binding at saturation. Inclusion of Triton X-100 and NaCl in the phosphate-buffered incubation medium prevented nonspecific adsorption to centrifuge tube walls, and gave lower but more reproducible specific binding results, respectively. An apparent dissociation constant of 5 . 10(-7) M and a binding density of 500 pmol toxin/mg membrane protein were derived from the saturation isotherms.
D000818:Animals; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004179:Cobra Cardiotoxin Proteins / Q000378:metabolism*; D004546:Elapid Venoms / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D051379:Mice; D009206:Myocardium / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology
D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms; D010664:Phenylmethylsulfonyl Fluoride