Comparative kinetic stabilities of staphylococcal enterotoxin types A, B, and C1.

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Comparative kinetic stabilities of staphylococcal enterotoxin types A, B, and C1.

Staphylococcal enterotoxin types A and C, were observed by viscosimetry and near-ultraviolet difference spectroscopy to unfold at concentrations of aqueous guanidine hydrochloride greater than 1 M. Apparent rate constants of unfolding calculated from spectral curves differed markedly for the two enterotoxins. Rate constants for the unfolding of enterotoxin A in 2 or 3 M guanidine hydrochloride ...

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Expression of staphylococcal enterotoxin C1 in Escherichia coli.

The structural gene encoding staphylococcal enterotoxin C1 was cloned into Escherichia coli and localized on a 1.5-kilobase HindIII-ClaI DNA fragment by subcloning. The toxin was partially purified from E. coli clones and shown to be immunologically identical to enterotoxin C1 from Staphylococcus aureus. The cloned toxin also had the same molecular weight (26,000) and charge heterogeneity as st...

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A DNA Spiegelmer to staphylococcal enterotoxin B.

Bacterial staphylococcal enterotoxin B is involved in several severe disease patterns and it was therefore used as a target for the generation of biologically stable mirror-image oligonucleotide ligands, so called Spiegelmers. The toxin is a 28 kDa protein consisting of 239 amino acids. Since the full-length protein is not accessible to chemical peptide synthesis, a stable domain of 25 amino ac...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1977

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)39924-6