Biological activities of the peptides of staphylococcal enterotoxin C formed by limited tryptic hydrolysis.

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Biological activity and complementation of the two peptides of staphylococcal enterotoxin B formed by limited tryptic hydrolysis.

Tryptic hydrolysis after reduction and carboxamidomethylation of staphylococcal enterotoxin B cleaved the single susceptible bond located between the 2 half-cystines of the molecule, Lys-Thr at positions 97 and 98 (Spero, L., Warren, J. R., and Metzger, J. F. (1973) J. Biol. Chem. 248, 7289-7294). The product remained as a single particle but was separated into the two constituent peptides by d...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1978

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)34246-1