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Mechanism of Activation of Adenylate Cyclase in vitro by Polymyxin-Released, Heat-Labile Enterotoxin of Escherichia coli

D. Michael Gill, Doyle J. Evans Jr. and Dolores G. Evans
The Journal of Infectious Diseases
Vol. 133, Supplement. The Structure and Functions of Enterotoxins (Mar., 1976), pp. S103-S107
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/30106736
Page Count: 5
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Mechanism of Activation of Adenylate Cyclase in vitro by Polymyxin-Released, Heat-Labile Enterotoxin of Escherichia coli
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Abstract

Heat-labile enterotoxic material released from Escherichia coli by polymyxin B activates the adenylate cyclase of pigeon erythrocyte ghosts in a time- and concentration-dependent manner. The activation requires nicotinamide adenine dinucleotide, adenosine triphosphate, and another component of the erythrocyte supernatant. The active species has a molecular weight of about 23,000-24,000 daltons, is inhibited by antibodies to the toxin of Vibrio cholerae, and is not irreversibly denatured by sodium dodecyl sulfate. Thus in many respects the active species from E. coli behaves the same as peptide A₁ of cholera toxin.

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