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Chemical modification of proteins to improve the accuracy of their relative molecular mass determination by electrophoresis
Author(s) -
Dolnik Vladislav,
Gurske William A.
Publication year - 2011
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201100141
Subject(s) - cationic polymerization , electrophoresis , capillary electrophoresis , chemistry , molecular mass , cytochrome c , chromatography , pulmonary surfactant , cytochrome , biochemistry , organic chemistry , mitochondrion , enzyme
Abstract We studied the electrophoretic behavior of basic proteins (cytochrome c and histone III) and developed a carbamylation method that normalizes their electrophoretic size separation and improves the accuracy of their relative molecular mass determined electrophoretically. In capillary zone electrophoresis with cationic hitchhiking, native cytochrome c does not sufficiently bind cationic surfactants due to electrostatic repulsion between the basic protein and cationic surfactant. Carbamylation suppresses the strong positive charge of the basic proteins and results in more accurate relative molecular masses.