Antibodies to heat-labile Escherichia coli enterotoxin in Apaches in Whiteriver, Arizona
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منابع مشابه
Antibodies to heat-labile Escherichia coli enterotoxin in Apaches in Whiteriver, Arizona.
Antitoxin titers to heat-labile Escherichia coli enterotoxin were measured in Apache children hospitalized with acute diarrhea and in Apaches of different age groups without diarrhea in Whiteriver, Ariz. The study suggests that in this locale, exposure to enterotocigenic E. coli is probably widespread and occurs early in life. Antitoxin titer rises after idarrheal disease associated with entero...
متن کاملHeat - 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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We report the complete DNA sequence of the Escherichia coli elt A gene, which codes for the A subunit of the heat-labile enterotoxin, LT. The amino acid sequence of the LT A subunit has been deduced from the DNA sequence of elt A. The LT A subunit starts with methionine, ends with leucine, and comprises 264 amino acids. The computed molecular weight of LT A is 29,673. The A subunit of cho...
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Chemically transformed mouse fibroblasts did not raise their cyclic AMP level in response to Escherichia coli heat-labile enterotoxin. These fibroblasts did, however, incorporate exogenous mono-, di-, and trisialogangliosides. After the uptake of monosialoganglioside galactosyl-N-acetylgalactosaminyl-[N-acetylneuraminyl]-galactosylglucosylceramide (GM1), the cells responded to E. coli heat-labi...
متن کاملCellular location of heat-labile enterotoxin in Escherichia coli.
We demonstrated that both the A and B subunits of heat-labile enterotoxin from Escherichia coli are located in the periplasm. The toxin was shown to form aggregates in Tris-EDTA buffers which are routinely used for isolating membranes. The aggregates pellet upon centrifugation, and this may explain why several previous investigators have concluded that enterotoxin is associated with membranes.
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1975
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.12.6.1475-1477.1975