Partial purification of acetylcholinesterase from the venom of the shore pit viper (Trimeresurus purpureomaculatus)

N H Tan; C S Tan

doi:10.1016/0041-0101(88)90190-0

Partial purification of acetylcholinesterase from the venom of the shore pit viper (Trimeresurus purpureomaculatus)

Toxicon. 1988;26(5):505-8. doi: 10.1016/0041-0101(88)90190-0.

Authors

N H Tan¹, C S Tan

Affiliation

¹ Department of Biochemistry, University of Malaya, Kuala Lumpur, Malaysia.

PMID: 3188057
DOI: 10.1016/0041-0101(88)90190-0

Abstract

Trimeresurus purpureomaculatus venom acetylcholinesterase has been partially purified by Sephadex G-200 gel filtration chromatography and DEAE Sephacel ion exchange chromatography. The enzyme has a mol. wt of 58,600. It was strongly inhibited by physostigmine salicylate and edrophonium chloride and exhibited substrate inhibition at high substrate concentration. The content of acetylcholinesterase in Trimeresurus purpureomaculatus venom was estimated to be much less than 0.3%.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acetylcholinesterase / isolation & purification*
Cholinesterase Inhibitors
Crotalid Venoms / analysis*
Substrate Specificity

Substances

Cholinesterase Inhibitors
Crotalid Venoms
Acetylcholinesterase