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J H Shaper

Publications and source records attributed to J H Shaper.

93 records · Page 6Linked to original sources

On the amino-acid sequence of flagellin from Bacillus subtilis 168: comparison with other bacterial flagellins.

A partial amino-acid sequence of Bacillus subtilis 168 flagellin is presented. The region of unassigned sequence in this 304-residue polypeptide chain spans residues 158-173. Comparison of the 27-residue aminoterminal CNBr peptide of B. subtilis 168 flagellin with that derived from the flagellin of the serologically unrelated strain of B. subtilis, W23, shows only three conservative substitutions, whereas the 16-residue carboxyl-terminal peptides derived from these flagellins were identical. The comparison of the very limited sequence information available on the flagellins of Salmonella and Proteus with that on B. subtilis indicates homology between these proteins.

Amino Acid Sequence↗

Effect of proteolytic enzymes on bacterial flagella.

Sheared flagella of Salmonella typhimurium strains SL 870 (Nml(+)Fla(+)) and SL 871 (Nml(-)Fla(+)) were found to be susceptible to proteolytic digestion by trypsin, chymotrypsin, and Pronase. The rate of tryptic digestion was similar for the epsilon-N-methyllysine-containing and the nonmethylated flagella. Thin fibers, which appeared to originate from only one end of the flagellar filament, were formed upon trypsin digestion. The fibers were not dissociated at extremes of pH or upon heating. The amino acid composition of the purified fibers was very different from that of intact Salmonella flagellin, and the fibers did not cross-react with antiflagellin or antiflagellar antiserum. The possible significance of these findings is discussed in relation to the flagellar structure.

Amino Acids↗