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Anal Biochem. 1999 May 1;269(2):399-402.

Mobility of acetylated histones in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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Departament de Bioquímica i Biologia Molecular, Universitat de València, València, Burjassot, E-46100, Spain.


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 epsilon-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.

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