Abstract
A neutral phospholipase A 2 (PLA 2) was separated from Pseudechis papuanus venom by a two-stage FPLC procedure of cation exchange and phenyl-Superose chromatography. It had a molecular mass of 15 kDa and a lower LD 50 value than a co-separated haemorrhagic fraction, indicating a higher lethal potency. In vitro tests confirmed the powerful inhibition of platelet aggregation by the PLA 2 and strong anticoagulant activity initially observed with whole venom. Ultrastructural studies showed that platelets lost their discoid shape and developed membranous projections with a general decrease in electron-density of the cytosol and disruption of the microfilaments following incubation with the enzyme. Amino acid sequence analysis of the N-terminus and some internal peptides demonstrated a high degree of homology with PLA 2s from other Pseudechis venoms. Our results indicate that this fraction is the main agent responsible for the haemostatic disorders in envenomed patients.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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