title: In vitro analysis of histone acetyltransferase activity.
abstract: Interest in histone acetylation has risen dramatically in recent years. In the following report, we present methods for the analysis of histone acetyltransferase activity in vitro. Protocols are described for radiolabeling histone proteins and N-terminal "tail" peptides, and for the analysis of acetylation by immunoblotting. Techniques for acetylating immobilized histone peptides are also described.
authors.affiliation: Biology Department, Boston College, 140 Commonwealth Ave., Chestnut Hill, MA 02467, USA.
authors.forename: Laura J
authors.initials: LJ
authors.lastname: Benson
authors.forename: Anthony T
authors.initials: AT
authors.lastname: Annunziato
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006367:HeLa Cells; D051548:Histone Acetyltransferases; D006657:Histones / Q000378:metabolism*; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*
chemical_list: D006657:Histones; D010446:Peptide Fragments; D000123:Acetyltransferases; D051548:Histone Acetyltransferases