Aislamiento y algunas propiedades de la proteinasa I del veneno de la serpiente peruana Lachesis muta.

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

2 Citas (Scopus)

Resumen

A proteolytic enzyme with high activity on casein was purified from Lachesis muta snake venom. This protein called "Proteinase I" was obtained using a gel filtration chromatography on Sephadex G-100 at pH 6.5, 0.1 M Ammonium acetate buffer, followed by ion exchange chromatography on DEAE-Cellulose at pH 7.5 and re-chromatographed on DEAE-Cellulose at pH 9.0 and 7.8 in Tris-HC1 buffer. A homogeneous band was obtained with the isolated protein on polyacrylamide gel electrophoresis. A molecular weight of 25,100 by gel filtration and an optimum pH of 8.4 were found for this enzyme. A total enzymatic activity was kept after a heating at 45 degrees C for ten minutes while the activity at 70 degrees C was 4% only. Synthetic esters as TAME and BAEE were not attacked by this enzyme. The activity was not affected by calcium ions and hemorrhagic action was not observed either.

Título traducido de la contribuciónIsolation and various properties of proteinase I from the venom of the Peruvian snake Lachesis muta
Idioma originalEspañol
Páginas (desde-hasta)219-225
Número de páginas7
PublicaciónActa Cientifica Venezolana
Volumen42
N.º4
EstadoPublicada - 1991
Publicado de forma externa

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