Snake venom phospholipases A2. A fluorescence study of their binding to phospholipid vesicles correlation with their anticoagulant activities.

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Snake venom phospholipases A2. A fluorescence study of their binding to phospholipid vesicles correlation with their anticoagulant activities.

The interaction of snake venom phospholipases A2 with phospholipids has been studied by intrinsic fluorescence. This has been performed in order to understand why some enzymes possess anticoagulant properties while others have no action on blood clotting. We show that phospholipases A2 can be distinguished according to their binding properties to phospholipid vesicles. Strong inhibitors of coag...

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Structural and Functional Characterization of Anticoagulant, FXa-binding Viperidae Snake Venom Phospholipases A2.

Certain snake venom phospholipases A2 (PLA2) have been identified as specific, non-competitive blood coagulation inhibitors that bind with high affinity to human activated blood coagulation factor X (hFXa). Recent determination of the three-dimensional structures of PLA2 isoforms which differ in anticoagulant activity contributes to a better understanding of their mode of binding to human FXa. ...

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Molecular Characterization of Lys49 and Asp49 Phospholipases A2 from Snake Venom and Their Antiviral Activities against Dengue virus

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Phospholipases A2: enzymatic assay for snake venom (Naja naja karachiensis) with their neutralization by medicinal plants of Pakistan.

Phospholipases A2 (PLA2) are the most lethal and noxious component of Naja naja karachiensis venom. They are engaged to induce severe toxicities after their penetration in victims. Present study was designed to highlight hydrolytic actions of PLA. in an egg yolk mixture and to encounter their deleterious effects via medicinal plants of Pakistan. PLA2 were found to produce free fatty acids in a ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1980

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)43892-1