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1: Arch Biochem Biophys. 1999 Jul 1;367(1):26-32.Click here to read Links

A novel phospholipase A2, BJ-PLA2, from the venom of the snake Bothrops jararaca: purification, primary structure analysis, and its characterization as a platelet-aggregation-inhibiting factor.

Serrano SM, Reichl AP, Mentele R, Auerswald EA, Santoro ML, Sampaio CA, Camargo AC, Assakura MT.

Laboratory of Biochemistry and Biophysics and Laboratory of Pathophysiology Instituto Butantan, São Paulo, 05503-900, Brazil. s_serrano@hotmail.com

This paper describes the isolation and primary structure analysis of a new phospholipase A2 with platelet-aggregation-inhibiting activity from the venom of Bothrops jararaca. The protein, named BJ-PLA2, was isolated by means of ammonium sulfate precipitation and anion-exchange and reversed-phase chromatographies and behaved as a homogeneous single-chain protein on SDS-PAGE. Its amino acid sequence was determined by N-terminal sequencing and analysis of overlapped chemical and proteolytic fragments by automated Edman degradation and mass spectometry determination. BJ-PLA2 consists of 124 amino acid residues and has the structural features of snake venom class II phospholipases A2. Chemical modification with p-bromophenacylbromide caused complete loss of enzymatic activity and partially affected the platelet-aggregation-inhibiting activity of BJ-PLA2. Copyright 1999 Academic Press.

PMID: 10375395 [PubMed - indexed for MEDLINE]