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• W1974815086 abstract "We describe an altered mobility for acetylated histone isoforms in sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Isoforms of histones H3 and H4 with a higher acetylation degree have a slightly faster electrophoretic mobility. Since acetylation neutralizes the positive charge of the ε-amino group of lysine, without significantly changing the molecular mass of the protein, the acetylation-dependent mobility shift could be explained by the increase of the net negative charge of the SDS–histone complexes. A possible consequence of this differential mobility for the acetylation site determination by protein microsequencing from SDS gels is discussed." @default.
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• W1974815086 date "1999-05-01" @default.
• W1974815086 modified "2023-09-28" @default.
• W1974815086 title "Mobility of Acetylated Histones in Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis" @default.
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• W1974815086 doi "https://doi.org/10.1006/abio.1999.4050" @default.
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