Phospholipase A2 electrophoretic variants in reptile venoms

J. P. Durkin, G. V. Pickwell, J. T. Trotter, W. T. Shier

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


The venoms of poisonous reptiles provide rich sources of phospholipase A2. We have investigated the potential usefulness of this enzyme in the characterization of venoms and in biochemical taxonomy of venomous reptiles using a recently developed electrophoretic technique. Venoms from Elapidae (18 species examined), especially Australian elapids (6), exhibited high phospholipase A2 activity and complex electrophoretic patterns. Dendroaspidae venoms (3) exhibited low or non-detectable phospholipase A2 activity in simple patterns. Viperidae venoms (5) yielded phospholipase A2 patterns with intermediate complexity and activity. Sea snake venoms (3) exhibited low phospholipase A2 activity and patterns of variable complexity. Crotalidae venoms (16) exhibited low or no detectable phospholipase A2 activity in simple patterns. The single colubrid venom examined yielded low phospholipase A2 activity and a simple electrophoretic pattern. Helodermatidae venoms (2) showed high activity with characteristic, complex patterns. In general, the venoms of snakes widely regarded as being more advanced exhibited phospholipase A2 patterns of lower complexity and activity. The complexity of the patterns obtained precludes extensive usefulness of the technique for taxonomy at the family and subfamily level, but it may make the technique useful for taxonomy at the subspecies level.

Original languageEnglish (US)
Pages (from-to)535-546
Number of pages12
Issue number4
StatePublished - 1981

Bibliographical note

Funding Information:
Ackrtowkdgenent~This research was supported in part by a fellowship from the National Research Council of Canada (toJ.P.D.), agrantfrom theCystic Fibrosis Foundation, National Science Foundation grant number PCM 80-11784, and private donations .


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