Biochemical and biological characterization of a PLA2 from crotoxin complex of Crotalus durissus cumanensis

Jaime Andrés Pereañez, Vitelbina Núñez, Salomón Huancahuire-Vega, Sergio Marangoni, Luis Alberto Ponce-Soto

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

43 Citas (Scopus)


A new PLA2 (Cdcum6) from crotoxin complex of Colombian Crotalus durissus cumanensis rattlesnake was purified using molecular exclusion chromatography and RP-HPLC. The molecular mass of Cdcum6 was determined by SDS-PAGE ∼14 KDa and confirmed by MALDI-TOF (14321.98 Da). The enzyme showed Km 6.0 mM, Vmax 3.44 nmol/min, optimum pH was 8.0 and temperature was between 30 and 45 °C, and it had a strict requirement of Ca2+ for its activity. The N-terminal sequence of PLA2 was SLVQF EKMIK EVAGK NGVPWY. Comparison of amino acid sequence data with other PLA2 from South American Crotalus durissus rattlesnakes showed that Cdcum6 shares the highest sequence identity with Cdr13 an isoform PLA2 from Crotalus durissus ruruima, nevertheless, Cdcum6 showed high content of basic and hydrophobic amino acids. In mice, Cdcum6 presented higher LD50 than crotoxin complex from C. d. cumanensis. Additionally, Cdcum6 induced a conspicuous local myotoxic effect and moderate footpad edema; in vitro, it was antigoagulant in doses as low as 0.5 μg/ml, and it was not cytotoxic on myoblast but Cdcum6 was able to lyse myotubes.

Idioma originalInglés
Páginas (desde-hasta)534-542
Número de páginas9
EstadoPublicada - abr. 2009
Publicado de forma externa


Profundice en los temas de investigación de 'Biochemical and biological characterization of a PLA2 from crotoxin complex of Crotalus durissus cumanensis'. En conjunto forman una huella única.

Citar esto