Sequence studies are presented on the cyanogen bromide peptides derived from the flagellin of Bacillus subtilis 168. Eight unique CNBr peptides, ranging in length from 4 to 113 residues, were isolated in pure state. These peptides accounted for the amino acid composition of flagellin. The NH2-terminal methionyl residue of the protein reacted only partially with CNBr. Partial cleavage was observed at a Met-Glu bond (residues 22 to 23) of the protein.
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