Characterization of mucrotoxin A from the venom of Trimeresurus mucrosquamatus (the Chinese habu snake).

Abstract

Mucrotoxin A from the venom of Trimeresurus mucrosquamatus was isolated in homogeneous form by a previously published method. Mucrotoxin A did not hydrolyze casein, however, when dimethylcasein was used as a substrate, the toxin cleaved the substrate. This toxin also hydrolyzed the oxidized B chain of insulin and fibrinogen. The sites of cleavage in the oxidized B chain of insulin were identified as Ser(9)-His(10), His(10)-Leu(11), Ala(14)-Leu(15), Leu(15)-Tyr(16) and Tyr(16)-Leu(17). The toxin digested the A alpha chain of fibrinogen first, followed by hydrolysis of the B beta chain. The fact that no fibrin clot formed indicates that the sites of cleavage in the A alpha and B beta chains of fibrinogen by the toxin must be different from those cleaved by thrombin. Mucrotoxin A produced systemic hemorrhage in internal organs such as the heart and stomach.

• Authors: M Kishida, T Nikai, N Mori, S Kohmura, H Sugihara
• Journal: Toxicon : official journal of the International Society on Toxinology (Toxicon) Vol. 23 Issue 4 Pg. 637-45 ( 1985) ISSN: 0041-0101 [Print] England
• PMID: 3904081 (Publication Type: Journal Article)

Chemical References

• Crotalid Venoms
• Trimeresurus venoms
• Creatine Kinase
• Peptide Hydrolases

Topics

• Animals
• Creatine Kinase (blood)
• Crotalid Venoms (analysis, toxicity)
• Hemorrhage (chemically induced)
• Mice
• Peptide Hydrolases (pharmacology)