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|Title:||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|
Reichl, A. P.
Auerswald, E. A.
Santoro, M. L.
Assakura, M. T.
Universidade Federal de São Paulo (UNIFESP)
Bothrops jararaca venom
primary structure analysis
|Publisher:||Academic Press Inc|
|Citation:||Archives of Biochemistry and Biophysics. San Diego: Academic Press Inc, v. 367, n. 1, p. 26-32, 1999.|
|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.|
|Appears in Collections:||Artigo|
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