Purification of Heat-Labile Enterotoxin from Escherichia coli 078:H11 by Affinity Chromatography with Antiserum to Vibrio cholerae Toxin
- 1 March 1976
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Infectious Diseases
- Vol. 133 (Supplement) , S138-S141
- https://doi.org/10.1093/infdis/133.supplement_1.s138
Abstract
Concentrated culture filtrate of Escherichia coli 078:H11, strain H10407, was applied to an affinity column prepared with IgG antibodies to the toxin of Vibrio cholerae. Elution of the retained material with 3 M KCNS yielded a nonenterotoxic protein that precipitated with antiserum to V. cholerae toxin and had three major protein components on sodium dodecyl sulfate gels. After treatment with 2-mercaptoethanol, two protein components were observed. Elution of the affinity column with 5 M guanidine yielded an enterotoxic protein that precipitated with antiserum to V. cholerae toxin. After treatment with 2-mercaptoethanol, only one protein component, with mobility identical to that of the slower component of the eluate (treated with 3 M KCNS and 2-mercaptoethanol), was observed.Keywords
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