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RESEARCH PRODUCT
Mobility of Acetylated Histones in Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis
Ramon SendraElena I. Georgievasubject
ErythrocytesSodiumLysineBiophysicschemistry.chemical_elementBiochemistryHistoneschemistry.chemical_compoundElectrochemistryAnimalsSodium dodecyl sulfateMolecular BiologyPolyacrylamide gel electrophoresisGel electrophoresisChromatographyMolecular massReproducibility of ResultsSodium Dodecyl SulfateAcetylationCell BiologyBlood Protein ElectrophoresisElectrophoresischemistryBiochemistryAcetylationElectrophoresis Polyacrylamide GelChickensdescription
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 e-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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-05-01 | Analytical Biochemistry |