The Primary Structure of Staphylococcal Enterotoxin B

Abstract

Abstract Thirty peptides obtained from the tryptic digestion of oxidized staphylococcal enterotoxin B were isolated chromatographically on columns of Dowex 50W-X2 and AG1-X2 by using pyridine-acetic acid and N-ethylmorpholine-pyridine-acetic acid buffer systems. The isolated peptides were further purified by paper chromatography and electrophoresis. The amino acid composition and sequence of each purified peptide were determined. A total of 239 amino acid residues was found to be present in the tryptic peptides.