title: Partial purification and some physicochemical properties of phospholipases A2 from the venom of the bushmaster snake (Lachesis muta).
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% 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.
authors.affiliation: Departamento de Bioquímica, Universidade Federal do Rio de Janeiro, Brasil.
authors.forename: A L
authors.initials: AL
authors.lastname: Fuly
authors.forename: I M
authors.initials: IM
authors.lastname: Francischetti
authors.forename: R B
authors.initials: RB
authors.lastname: Zingali
authors.forename: C R
authors.initials: CR
authors.lastname: Carlini
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D010741:Phospholipases A / Q000302:isolation & purification* / Q000494:pharmacology; D054467:Phospholipases A2; D010974:Platelet Aggregation; D014757:Viper Venoms / Q000737:chemistry* / Q000201:enzymology / Q000378:metabolism; D017819:Viperidae
chemical_list: D014757:Viper Venoms; D010741:Phospholipases A; D054467:Phospholipases A2