Mobility of acetylated histones in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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.
Georgieva
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Departament de Bioquímica i Biologia Molecular, Universitat de València, València, Burjassot, E-46100, Spain.
Sendra
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D000107:Acetylation; D000818:Animals; D001797:Blood Protein Electrophoresis / Q000379:methods / Q000706:statistics & numerical data; D002645:Chickens; D004563:Electrochemistry; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods* / Q000706:statistics & numerical data; D004912:Erythrocytes / Q000737:chemistry; D006657:Histones / Q000097:blood / Q000737:chemistry / Q000302:isolation & purification*; D015203:Reproducibility of Results; D012967:Sodium Dodecyl Sulfate
D006657:Histones; D012967:Sodium Dodecyl Sulfate