Aislamiento y algunas propiedades de la toxina Be1 del veneno de Brachistosternus ehrenbergii (Gervais, 1841) (Scorpiones:Bothriuridae)

Translated title of the contribution: Isolation and some properties of Be1 toxin from the venom of Brachistosternus ehrenbergii (Gervais, 1841) (Scorpiones:Bothriuridae)

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3 Scopus citations

Abstract

By means of cationic exchange chromatography on CM-Sephadex C-25 column (16 × 1,1 cm) with ammonium acetate buffer 0,05 M at pH 7, from Brachistosternus ehrenbergii scorpion venom was isolated a protein with toxic activity on mice. In this system the toxin was ligated to gel and was eluated with buffer and NaCl 0,6M. The toxin denominated Be1 and it characterizes to be a basic protein that constitute 8,1% of venom total protein. Toxin purity was evaluated by electrophoresis in natives conditions, according to Reisfeld-method, and denaturants conditions by the Schagger-and-von Jagow-method, the toxin is a single chain polypeptide of 6,3 kDa has been determined. The inoculation of 60 μg toxin on albino mice, intraperitoneal way, produces some local signals as salival hipersecretion followed by respiratory affection, drags hind feet and finally 2 hours after, death. Intramuscular way (7,6 μg) Be1 produces temporal paralysis of the inoculated limb. The toxin has neither phospholipase, nor protease, nor acetylcholinesterase nor acetylcholinesterase inhibitor activity.

Translated title of the contributionIsolation and some properties of Be1 toxin from the venom of Brachistosternus ehrenbergii (Gervais, 1841) (Scorpiones:Bothriuridae)
Original languageSpanish
Pages (from-to)243-247
Number of pages5
JournalRevista Peruana de Biologia
Volume13
Issue number3
StatePublished - Jul 2007
Externally publishedYes

Bibliographical note

Funding Information:
El trabajo contó con el financiamiento del Consejo Superior de Investigaciones de la Universidad Nacional Mayor de San Marcos (Proyectos 031001211 y 041001221).

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