Abstract
AbstractSix hemorrhagic toxins have been isolated from Crotalus atrox (western diamondback rattlesnake) venom. All of them contain one mole of zinc per mole of protein, although the molecular weights vary from 24,000 to 68,000. All have proteolytic activity when tested on dimethyl-casein. Removal of zinc eliminates the hemorrhagic and proteolytic activities. Proteolytic specificity of hemorrhagic toxin a is highly specific and hydrolyzes the X-Leu bond. Hemorrhagic toxin b is less specific and hydrolyzes the X-Phe, X-Ser, and X-Leu bonds.There are several types of myonecrotic [muscle damaging) toxins, and of those, myotoxin a from C. viridis viridis (prairie rattlesnake) venom is the most extensively investigated. Myotoxin a consists of 42 amino acid residues with 3 disulfide bonds. There is no similarity in amino acid sequence and disulfide bond positions when compared to well-known post-synaptic neurotoxins (both Type I and II) of snake venoms. It is rather curious and interesting to note that there is ...
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
