title: Mobility of acetylated histones in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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 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.
authors.affiliation: Departament de Bioquímica i Biologia Molecular, Universitat de València, València, Burjassot, E-46100, Spain.
authors.forename: E I
authors.initials: EI
authors.lastname: Georgieva
authors.forename: R
authors.initials: R
authors.lastname: Sendra
mesh_terms: 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
chemical_list: D006657:Histones; D012967:Sodium Dodecyl Sulfate