Section 11
Chapter 10,084

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, S.M.; Reichl, A.P.; Mentele, R.; Auerswald, E.A.; Santoro, M.L.; Sampaio, C.A.; Camargo, A.C.; Assakura, M.T.

Archives of Biochemistry and Biophysics 367(1): 26-32


ISSN/ISBN: 0003-9861
PMID: 10375395
DOI: 10.1006/abbi.1999.1230
Accession: 010083370

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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.

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