Abstract
Extracellular proteins produced by Bacillus cereus AL-42 and AL-15 were fractioned by chromatography on QAE-Sephadex and Sephadex G75. This last chromatographic process resulted in three peaks. The major peak showed vascular permeability activity to rabbits, lethality to mice, and cytotoxicity to Vero and Hela cells. The analysis by SDS-PAGE after ultrafiltration confirm recent findings that the enterotoxin is a compound with molecular mass > 30.000.
Bacilus cereus; enterotoxin; toxic fator; purification
Partial isolation and some properties of enterotoxin produced by Bacillus cereus strains
T. V. Guaycurus1
A. C. Vicente2
S. Giovanni De Simone3
L. Rabinovitch1
Instituto Oswaldo Cruz, Departamento de Bacteriologia, Rio de Janeiro, Brasil
Instituto Oswaldo Cruz, Departamento de Genética, Rio de Janeiro, Brasil
Instituto Oswaldo Cruz, Departamento de Bioquímica e Biologia Molecular, Rio de Janeiro, Brasil
Extracellular proteins produced by Bacillus cereus AL-42 and AL-15 were fractioned by chromatography on QAE-Sephadex and Sephadex G75. This last chromatographic process resulted in three peaks. The major peak showed vascular permeability activity to rabbits, lethality to mice, and cytotoxicity to Vero and Hela cells. The analysis by SDS-PAGE after ultrafiltration confirm recent findings that the enterotoxin is a compound with molecular mass > 30.000.
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Publication Dates
-
Publication in this collection
01 June 2009 -
Date of issue
Mar 1993
