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• W1884555802 abstract "Various disulfide-reducing agents, mostly thiols and thiol precursors, were examined for their ability to reduce the disulfide bonds in the Escherichia coli heat-stable enterotoxin STa; reduction of the bonds results in loss of biological activity. The biological activity measured was the stimulation of guanylate cyclase in pig intestinal brush border membranes by STa. Nearly all of the compounds inactivated STa, although at different rates; a smaller number appreciably decreased guanylate cyclase activity when they were introduced into the reaction mixture after STa bound to its receptor. With dithiothreitol, the decrease in reaction rate was both time and concentration dependent and resulted in a reversal to basal activity. The anionic thiols were relatively ineffective in reversing activation, the neutral monothiols were moderately effective, and the aminothiols and neutral dithiols were the most effective. The order of effectiveness of the compounds was S-2-(3-aminopropylamino)ethanethiol greater than 2,3-dimercaptopropanol = 2-aminoethylisothiuronium bromide greater than dithiothreitol greater than 2-mercaptoethylamine greater than alpha-thioglycerol. These compounds were used in weanling pig ligated-intestinal-loop bioassays to determine if STa-induced secretion was reduced when they were injected 20 min after the STa. Instead of S-2-(3-aminopropylamino)ethanethiol we used the phosphorylated derivative S-2-(3-aminopropylamino)ethylphosphorothioic acid; this compound and 2,3-dimercaptopropanol were the only compounds that reduced STa-induced secretion and had no direct secretory or pathological effects." @default.
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• W1884555802 date "1986-01-01" @default.
• W1884555802 modified "2023-09-26" @default.
• W1884555802 title "Reversal of the biological activity of Escherichia coli heat-stable enterotoxin by disulfide-reducing agents" @default.
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• W1884555802 doi "https://doi.org/10.1128/iai.51.1.24-30.1986" @default.
• W1884555802 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/261060" @default.
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