PARTIAL-PURIFICATION AND SOME PHYSICOCHEMICAL PROPERTIES OF PHOSPHOLIPASES-A(2) FROM THE VENOM OF THE BUSHMASTER SNAKE (LACHESIS-MUTA)

Screening of the biochemical-pharmacological properties of the crude v enom from the snake Lachesis muta indicated the presence of phospholip ase A2 (PLA2; 5260 U/mg protein), procoagulant (2630 U/mg protein), pl atelet aggregating (43 U/mg protein) and caseinolytic activities (6670 U/mg protein). These activities were separated by filtration of the c rude venom on Sephacryl S-200. The material containing PLA2 activity w as further fractioned by DEAE-cellulose ion exchange chromatography in to four active fractions (F-I to F-IV, containing 1.7, 1.2, 0.3, and 0 .05% of the crude venom protein, respectively) by stepwise elution wit h buffers of increasing ionic strength. All fractions presented a mole cular weight of approximately 15,000 and isoelectric points in the ran ge pH 4.6-6.0. In addition to their indirect hemolytic activity, the p artially purified fractions inhibited platelet aggregation induced eit her by collagen or thrombin. p-Bromophenacyl bromide-treated fractions lost both phospholipase A2 activity and their inhibitory effect on co llagen-induced platelet aggregation.