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 Gowda, T. Veerabasappa (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. ISSN 0041-0101

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Abstract

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.

Item Type: Article
Additional Information: Unmapped bibliographic data: PY - 1994/10// [EPrints field already has value set] JO - Toxicon [Field not mapped to EPrints]
Subjects: Agriculture Biological Sciences > Biochemistry
University of Mysore > PG Campuses > Manasagangotri, Mysore > Agriculture Biological Sciences > Biochemistry
Divisions: PG Campuses > Manasagangotri, Mysore > Biochemistry
Depositing User: Swamy D
Date Deposited: 12 Jul 2013 05:48
Last Modified: 11 Sep 2013 06:03
URI: http://eprints.uni-mysore.ac.in/id/eprint/13740

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