PURIFICATION OF A BASIC PHOSPHOLIPASE A(2) FROM INDIAN SAW-SCALED VIPER (ECHIS-CARINATUS) VENOM - CHARACTERIZATION OF ANTIGENIC, CATALYTIC AND PHARMACOLOGICAL PROPERTIES

A major basic phospholipase A(2) was purified from the Indian saw-scaled viper (Echis carinatus) venom by the combination of column chromatography and electrophoresis. The purified phospholipase A(2) (EC-IV-PLA(2)) has a mel. wt of 14,000 by SDS-PAGE. It is a basic protein with a pI value between 7.2 and 7.6, and has a fluorescence emission maxima at 340 nm. It induces neurotoxicity and oedema in mice with an i.p. LD(50) Of 5 mg/kg body weight. It is devoid of direct haemolytic, myotoxic, cytotoxic and anticoagulant activities. Rabbit polyclonal antibodies prepared against EC-IV-PLA(2) inhibited the in vitro enzymatic activity dose dependently, but did not neutralize the toxic effects of EC-IV-PLA(2) in experimental animals.