Structural Characterisation of the E. coli Heat Stable Enterotoxin STh
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چکیده
منابع مشابه
Structural 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...
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 کاملSelective targeting of E. coli heat-stable enterotoxin analogs to human colon cancer cells.
BACKGROUND Radiolabeled analogs of the E. coli heat-stable enterotoxin (ST(h)) are currently under study as imaging and therapeutic agents for colorectal cancer. The aim of these studies is to compare in vitro and in vivo characteristics of two novel ST(h) analogs with appended DOTA chelating moieties. MATERIALS AND METHODS ST(h) analogs were synthesized with pendant N-terminal DOTA moieties ...
متن کاملProtection 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...
متن کاملEnzyme-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: The Open Spectroscopy Journal
سال: 2009
ISSN: 1874-3838
DOI: 10.2174/1874383800802010034