Partial purification and some physicochemical properties of phospholipases A2 from the venom of the bushmaster snake (Lachesis muta)
Braz. j. med. biol. res
; 26(5): 459-63, May 1993. graf
Article
em En
| LILACS
| ID: lil-148699
Biblioteca responsável:
BR1.1
ABSTRACT
Screening of the biochemical-pharmacological properties of the crude venom from the snake Lachesis muta indicated the presence of phospholipase A2 (PLA2; 5260 U/mg protein), procoagulant (2630 U/mg protein), platelet aggregating (43 U/mg protein) and caseinolytic activities (6670 U/mg protein). These activities were separated by filtration of the crude venom on Sephacryl S-200. The material containing PLA2 activity was further fractioned by DEAE-cellulose ion exchange chromatography into four active fractions (F-I to F-IV, containing 1.7, 1.2, 0.3, and 0.05 per cent of the crude venom protein, respectively) by stepwise elution with buffers of increasing ionic strength. All fractions presented a molecular weight of approximately 15,000 and isoelectric points in the range pH 4.6-6.0. In addition to their indirect hemolytic activity, the partially purified fractions inhibited platelet aggregation induced either by collagen or thrombin. p-Bromophenacyl bromide-treated fractions lost both phospholipase A2 activity and their inhibitory effect on collagen-induced platelet aggregation
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Coleções:
01-internacional
Base de dados:
LILACS
Assunto principal:
Fosfolipases A
/
Venenos de Víboras
Limite:
Animals
Idioma:
En
Revista:
Braz. j. med. biol. res
Assunto da revista:
BIOLOGIA
/
MEDICINA
Ano de publicação:
1993
Tipo de documento:
Article
/
Congress and conference
País de publicação:
Brasil