Snake venom cardiotoxin induces G-actin polymerization.
Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl2 was present in the buffer and could be inhibited if G-actin was preincubated with deoxyribonuclease I. Furthermore, the DNAase could also partially depolymerize actin polymer previously formed by the interaction of G-actin with the toxin.
Chen
Y H
YH
Institute of Biochemical Sciences, College of Sciences, National Taiwan University, Taipei, China.
Chu
S T
ST
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001704:Biopolymers / Q000378:metabolism; D004179:Cobra Cardiotoxin Proteins / Q000494:pharmacology*; D004546:Elapid Venoms / Q000494:pharmacology*; D066298:In Vitro Techniques; D009132:Muscles / Q000187:drug effects / Q000378:metabolism; D011817:Rabbits
D000199:Actins; D001704:Biopolymers; D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms