The susceptibility to tryptic hydrolysis of peptide bonds involving epsilon-N-methyllysine.
Using isolation of soluble peptides as a means of comparing the efficiency of tryptic hydrolysis of various forms of the phase-1 flagellin of Salmonella typhimurium, it was found that peptides terminating in N-methyllysine required a longer period of exposure to enzyme for their detection than did equivalent peptides terminating in lysine.
D001426:Bacterial Proteins; D005408:Flagellin; D008239:Lysine / Q000031:analogs & derivatives*; D010446:Peptide Fragments / Q000032:analysis; D012482:Salmonella paratyphi A / Q000032:analysis*; D013045:Species Specificity; D014357:Trypsin
D001426:Bacterial Proteins; D010446:Peptide Fragments; C005205:epsilon-N-methyllysine; D005408:Flagellin; D014357:Trypsin; D008239:Lysine