title: Localization of lysines acetylated in ubiquitin reacted with p-nitrophenyl acetate.
abstract: The protein ubiquitin undergoes extensive N epsilon-acetylation of some of its seven lysine residues when reacted with p-nitrophenyl acetate. Lysines 27 and 29 show little reactivity whereas residue 6 is the most readily acetylated. Residues 11, 33, 48, and 63 show intermediate reactivities.
authors.forename: J R
authors.initials: JR
authors.lastname: Jabusch
authors.forename: H F
authors.initials: HF
authors.lastname: Deutsch
mesh_terms: D000107:Acetylation; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002021:Buffers; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004589:Electrophoresis, Disc; D006609:High Mobility Group Proteins; D006736:Horses; D008239:Lysine / Q000031:analogs & derivatives* / Q000032:analysis; D008314:Malonates; D009596:Nitrophenols; D010446:Peptide Fragments / Q000032:analysis; D014452:Ubiquitins
chemical_list: D000596:Amino Acids; D002021:Buffers; D006609:High Mobility Group Proteins; D008314:Malonates; D009596:Nitrophenols; D010446:Peptide Fragments; D014452:Ubiquitins; C016949:N-epsilon-acetyllysine; C008642:4-nitrophenyl acetate; D008239:Lysine; C030978:diethylmalonic acid