Purification of a basic phospholipase A2 from Indian saw-scaled viper (Echis carinatus) venom: characterization of antigenic, catalytic and pharmacological properties

Kemparaju, K. and Nijaguna Prasad, B. and Veerabasappa Gowda, T. (1994) Purification of a basic phospholipase A2 from Indian saw-scaled viper (Echis carinatus) venom: characterization of antigenic, catalytic and pharmacological properties. Toxicon, 32 (10). pp. 1187-1196.

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Official URL: https://doi.org/10.1016/0041-0101(94)90348-4

Abstract

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.

Item Type: Article
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Biochemistry
Depositing User: Users 23 not found.
Date Deposited: 03 May 2021 06:32
Last Modified: 07 Jul 2022 09:51
URI: http://eprints.uni-mysore.ac.in/id/eprint/16227

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