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[Mobility on peptide maps of peptides obtained by tryptic hydrolysis of lysozyme oxidized at the S-S-bonds].

The peptide map obtained by tryptic hydrolysis of the lysozyme oxidized at the S--S-bonds was characterized and compared with that of tryptic hydrolysis of the reduced lysozyme. It was shown that the mobility of peptides containing oxidized amino acid residues is decreased under electrophoresis and chromatographic treatment. Under a decrease in the peptide charge during oxidation, the changes in electrophoretic and chromatographic mobilities show a correlation. In case when the peptide charge remains unchanged, only chromatographic mobility may be altered. It is demonstrated that the cystein residues significantly interfere with the effects of trypsin on the adjacent bonds.