Purification of a basic phospholipase A2 from Indian saw-scaled viper (Echis carinatus) venom: characterization of antigenic, catalytic and pharmacological properties.
A major basic phospholipase A2 was purified from the Indian saw-scaled viper (Echis carinatus) venom by the combination of column chromatography and electrophoresis. The purified phospholipase A2 (EC-IV-PLA2) has a mol. 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. LD50 of 5 mg/kg body weight. It is devoid of direct haemolytic, myotoxic, cytotoxic and anticoagulant activities. Rabbit polyclonal antibodies prepared against EC-IV-PLA2 inhibited the in vitro enzymatic activity dose dependently, but did not neutralize the toxic effects of EC-IV-PLA2 in experimental animals.
Department of Studies in Biochemistry, University of Mysore, Manasa Gangothri, India.
K
K
Kemparaju
B N
BN
Prasad
V T
VT
Gowda
D000818:Animals; D000918:Antibody Specificity; D002850:Chromatography, Gel; D004305:Dose-Response Relationship, Drug; D004487:Edema / Q000139:chemically induced; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007106:Immune Sera / Q000276:immunology; D007074:Immunoglobulin G / Q000276:immunology; D007525:Isoelectric Focusing; D007928:Lethal Dose 50; D008297:Male; D051379:Mice; D008970:Molecular Weight; D009498:Neurotoxins / Q000633:toxicity; D009500:Neutralization Tests; D010741:Phospholipases A / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification* / Q000633:toxicity; D054467:Phospholipases A2; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014757:Viper Venoms / Q000201:enzymology*
D007106:Immune Sera; D007074:Immunoglobulin G; D009498:Neurotoxins; D014757:Viper Venoms; D010741:Phospholipases A; D054467:Phospholipases A2