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Título : Puri¢cation and characterisation of a haemorrhagic fraction from the venom of the Uracoan rattlesnake Crotalus vegrandis
Autor : Aguilar, Irma
Giron, Maria E
Rodríguez-Acosta, Alexis
Palabras clave : Crotalidae
Haemorrhagic fraction
Crotalus vegrandis
Fecha de publicación : 27-Nov-2013
Citación : Biochimica et Biophysica Acta;1548 (2001) 57-65
Resumen : Uracoan rattlesnake (Crotalus vegrandis) venom was subjected to chromatographic, electrophoretic, biochemical and in vivo haemorrhagic analysis. A haemorrhagic toxin (Uracoina-1) active on skin at the site of inoculation in mice was purified by Mono Q2 anion-exchange chromatography and size exclusion (SE) high-performance liquid chromatography. The purified preparation was a protein of Mr 58 000 as revealed by sodium dodecyl sulphate^polyacrylamide gel electrophoresis under denatured conditions and with silver staining. The use of EDTA, EGTA and 1,10-phenanthroline inhibited haemorrhagic and proteolytic activities. Inhibitors of serine proteinases such as PMSF and TCLK had no effect on the haemorrhagic fraction. Uracoina-1 hydrolyses casein, hide powder azure and fibrinogen have an optimal pH of 8.2. It rapidly digests the AK-chain of fibrinogen. Thermal denaturation of Uracoina-1 after exposure at 60³C for 15 min led to inactivation of the haemorrhagic activity. In addition, Uracoina-1 is myotoxic, lacking haemolytic, defibrinating and lethal effects. The N-terminal amino acid sequence (20 residues) was determined.
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