Escherichia coli heat-labile enterotoxin. Ganglioside specificity and ADP-ribosyltransferase activity.

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Escherichia coli heat-labile enterotoxin. Ganglioside specificity and ADP-ribosyltransferase activity.

Escherichia coli heat-labile enterotoxin (LT) bound to rat glioma C6 cells that had incorporated ganglioside GMl but not to cells that had taken up gangliosides GM2, GD~, or G D ~ ~ . The same specificity also was observed with choleragen, the enterotoxin of Vihrio cholem. The tryptophanyl fluorescence spectra of LT and its B component differed from those of choleragen and its B component, resp...

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Activation of adenylate cyclase by heat-labile Escherichia coli enterotoxin. Evidence for ADP-ribosyltransferase activity similar to that of choleragen.

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Takai, Y., Kishimoto, A,, Kawahara, Y., Minakuchi, R.. Sano, K., Kikkawa, U., Mori, T., Yu, B., Kaibuchi, K. & Nishizuka, y. (1981) Adv. Cyclic Nucleotide Res. 14, 301-313 Thomas, D. D. & Knoop, F. C. (1982) J. Inject Dis. 145, 141147 Thomas, D. D. & Knoop, F. C. (1983) J . Infect. Dis. 147,450-459 Turnberg, L. A., Bieberdorf, F. A,, Morawski, S. G . & Fordtran, J. S. (1970) J. Clin. Invest. 49...

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Heat - labile Enterotoxin of Escherichia coli

Heat-labile enterotoxin (LT) was obtained in large quantities (several-gram amounts) and great purity from Escherichia coli C600 carrying the LT-coding multicopy plasmid EWD299. By growing this strain on a medium that allows high cell densities in the early stationary phase, we increased the net LT production per milliliter by a factor of 200, compared to natural porcine enterotoxigenic E. coli...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1981

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)42975-4