Citation

Dhananjaya BL, d'Souza CJM. Basic Clin. Pharmacol. Toxicol. 2011; 108(2): 79-83.

Affiliation

Department of Studies in Biochemistry, University of Mysore, Manasagangothri, Mysore, India Department of Biochemistry and molecular Biology, central University of Kerala, Kasargoud, Kerala, India.

Copyright

(Copyright © 2011, Nordic Pharmacological Society, Publisher John Wiley and Sons)

DOI

10.1111/j.1742-7843.2010.00630.x

PMID

21156030

Abstract

  Snake venom components, acting in concert in the prey, cause their immobilization and initiate digestion. To achieve this, several hydrolytic enzymes of snake venom have evolved to interfere in various physiological processes, which are well defined. However, hydrolytic enzymes such as phosphatases (acid and alkaline phosphomonoesterases) are less studied and their pharmacological role in venoms is not clearly defined. Also, they show overlapping substrate specificities and have other common biochemical properties causing uncertainty about their identity in venoms. The near-ubiquitous distribution of these enzymes in venoms, suggests a significant role for these enzymes in envenomation. It appears that these enzymes may play a central role in liberating purines (mainly adenosine) - a multitoxin and through the action of purines help in prey immobilization. However, apart from this, these enzymes could also possess other pharmacological activities as venom enzymes have been evolved to interfere in diverse physiological processes. This has not been verified by pharmacological studies using purified enzymes. Further research is needed to biologically characterize these enzymes in snake venoms, such that their role in venom is clearly established.

Language: en