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

Translated title of the contribution: Isolation and various properties of proteinase I from the venom of the Peruvian snake Lachesis muta

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Abstract

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.

Translated title of the contributionIsolation and various properties of proteinase I from the venom of the Peruvian snake Lachesis muta
Original languageSpanish
Pages (from-to)219-225
Number of pages7
JournalActa Cientifica Venezolana
Volume42
Issue number4
StatePublished - 1991
Externally publishedYes

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