Biochemical Properties of Escherichia coli Low-Molecular-Weight, Heat-Stable Enterotoxin

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Biochemical 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...

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Properties 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...

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Polymyxin B-Induced Release of Low-Molecular-Weight, Heat-Labile Enterotoxin from Escherichia coli.

Polymyxin B-induced release of enterotoxin from Escherichia coli strain H-10407 was demonstrated. Incubation of E. coli cells derived from 6-h cultures with polymyxin caused the rapid release of enterotoxin with a molecular weight of approximately 20,000, as estimated by the gel filtration technique. The rapidity of the release of enterotoxin indicates that it probably resides in the periplasmi...

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Protection in rats immunized with Escherichia coli heat-stable enterotoxin.

Rats immunized with a semipurified preparation of the Escherichia coli heat-stable (ST) enterotoxin conjugated with a protein carrier were protected against challenge with semipurified or purified ST and viable organisms of multiple heterologous serotypes that produce only ST (LT-/ST+), but they were not protected against heal-labile (LT) toxin or viable strains which produce LT either alone (L...

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Enzyme-linked immunosorbent assay for Escherichia coli heat-stable enterotoxin.

The sensitivity of an enzyme-linked immunosorbent assay (ELISA) to detect pure native Escherichia coli heat-stable toxin (ST) and to identify ST-producing strains among clinical isolates was determined. Two synthetically produced ST preparations were used to raise hyperimmune antisera in rabbits and goats: ST(S), which has the same antigenicity as native ST; and ST(C), which is 15-fold more imm...

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ژورنال

عنوان ژورنال: Infection and Immunity

سال: 1974

ISSN: 0019-9567,1098-5522

DOI: 10.1128/iai.9.2.342-347.1974