Immunological properties of purified Klebsiella pneumoniae heat-stable enterotoxin
نویسندگان
چکیده
منابع مشابه
Purification and properties of Klebsiella pneumoniae heat-stable enterotoxin.
The enterotoxic material in cell-free growth preparations of Klebsiella pneumoniae serotype 5 was purified by sequential ultrafiltration and gel filtration (GF) procedures and the fractions were assayed for enterotoxic activity by determining their ability to induce in vivo net water secretion in the rat jejunum. Whole-cell lysates were inactive. Anaerobic broth culture conditions yielded a 10-...
متن کاملProperties of synthetically produced Escherichia coli heat-stable enterotoxin.
The properties of a synthetically produced peptide composed of the same primary structure of 18 amino acids described for human Escherichia coli heat-stable enterotoxin were compared with those of purified heat-stable toxin obtained by bacterial growth. The dosage required to evoke fluid secretion in the suckling mouse and rat ligated ileal loop assays was the same for both toxins. The antigeni...
متن کاملPlasmid-mediated properties of a heat-stable enterotoxin-producing Escherichia coli associated with infantile diarrhea.
The plasmid mediation and transmissibility of heat-stable enterotoxin production and multiple antibiotic resistance have been demonstrated for Escherichia coli O78:K80:H12 epidemiologically incriminated in a hospital outbreak of infantile diarrhea. The conjugal transfer of a 67 X 10(6) - and a 30 X 10(6)-dalton plasmid was associated with the transfer of resistances and enterotoxin production, ...
متن کاملBiochemical properties of Escherichia coli low-molecular-weight, heat-stable enterotoxin.
The low-molecular-weight, heat-stable type of Escherichia coli enterotoxin (ST) was obtained from sterile syncase broth filtrates of human and animal enteropathogenic E. coli strains. ST was assayed in infant mice, and it was found that this assay was specific for ST in that the high-molecular-weight, heat-labile type of E. coli exterotoxin would not cause fluid accumulation in these animals. S...
متن کاملStructural Characterisation of the E. coli Heat Stable Enterotoxin STh
E. coli heat stable enterotoxin STa is an agonist of the membrane guanylate cyclase C whose endogenous ligands are the peptide hormones guanylin and uroguanylin. Whereas these peptides contain only two disulfide bonds, STa is stabilized by one additional disulfide bridge. We chemically synthesized the enterotoxin STh that originates from the E. coli strain found in humans, and we determined its...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1983
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.42.2.838-841.1983