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

Abstract

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. (C) 1999 Academic Press.Inst Butantan, Biochem & Biophys Lab, BR-05503900 São Paulo, BrazilInst Butantan, Lab Pathophysiol, BR-05503900 São Paulo, BrazilUNIFESP, Dept Biochem, São Paulo, BrazilUniv Munich, Klinikum Innenstadt, Dept Clin Chem & Clin Biochem, D-80336 Muenchen, GermanyUNIFESP, Dept Biochem, São Paulo, BrazilWeb of Scienc