Chentsova T V, Kravchenko N A
Biokhimiia. 1978 Nov;43(11):1977-82.
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.
对经二硫键氧化的溶菌酶进行胰蛋白酶水解所得到的肽图进行了表征，并与还原型溶菌酶的胰蛋白酶水解肽图进行了比较。结果表明，含有氧化氨基酸残基的肽在电泳和色谱处理下迁移率降低。在氧化过程中肽电荷减少时，电泳迁移率和色谱迁移率的变化呈现相关性。当肽电荷保持不变时，可能只有色谱迁移率会改变。结果表明，半胱氨酸残基会显著干扰胰蛋白酶对相邻肽键的作用。
