Identification of Enterotoxin E

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Identification of enterotoxin E.

Identification of a new enterotoxin was accomplished by purification of the enterotoxin produced by staphylococcal strain FRI-326 and by preparation of specific antitoxin to the enterotoxin. Toxicity of the preparations was determined in rhesus monkeys, and specificity of the enterotoxin-antitoxin reaction was determined in gel diffusion plates. The enterotoxin was designated enterotoxin E.

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Detection of Staphylococcus Aureus Enterotoxin Genes A-E

Abstract Background and Objective: The main cause of spreading staphylococcal infections among patients is the healthy carriers working in hospitals. With the secretion of different sorts of toxins such as entrotoxin, this bacteria can provide the conditions for attacking on the host. The main objective of this study is identification of the characteristics and differences in the Staphylococc...

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Identification of the classical enterotoxin genes of Staphylococcus aureus in various foods by multiplex PCR assay

Background: An annual update of information about the prevalence of Staphylococcus aureus and staphylococcal enterotoxins (SEs) genes is required in every geographic area. Aims: This study was conducted to investigate the prevalence of the bacterium and type of associated enterotoxin genes in different food samples, using multiplex polymerase ...

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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...

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Purification and some physicochemical properties of staphylococcal enterotoxin E.

Enterotoxin E produced by Stu~hyZococcus aureus strain FRI (Food Research Institute)-326 was purified by cation exchange chromatography on carboxymethylcellulose, gel tiltration through superfine Sephadex G-75, and gel filtration in 6 M urea with superfine Sephadex G-75. The purified toxin appears to be nearly homogeneous by paper, starch gel, and polyacrylamide gel electrophoresis and double g...

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ژورنال

عنوان ژورنال: Infection and Immunity

سال: 1971

ISSN: 0019-9567,1098-5522

DOI: 10.1128/iai.4.5.593-595.1971