Biochemical and electrophysiological characteristics of toxins isolated from the venom of the scorpion Centruroides sculpturatus.
Recent progress in biochemical, structural and physiological studies has revealed several interesting properties of the toxins from the American scorpion, Centruroides sculpturatus. These toxins, together with similar toxins from other species of scorpions, comprise a unique family of homologous proteins with phylogenetically related structural differences. There is now evidence from both binding and electrophysiological studies that two distinct classes of toxins are present in the venom of C. sculpturatus. One class of toxins markedly slows inactivation of the sodium permeability but has no demonstrable effect on activation, whereas the second class induces a transient shift in the voltage-dependence of activation. Both groups make inactivation incomplete.
D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography; D004594:Electrophysiology; D007473:Ion Channels / Q000187:drug effects; D009498:Neurotoxins / Q000302:isolation & purification*; D011487:Protein Conformation; D011901:Ranvier's Nodes / Q000187:drug effects / Q000503:physiopathology; D012604:Scorpion Venoms / Q000302:isolation & purification*; D012964:Sodium / Q000378:metabolism
C035413:Centruroides toxin; D007473:Ion Channels; D009498:Neurotoxins; D012604:Scorpion Venoms; D012964:Sodium