title: Human red cell acetyltransferase.
abstract: Acetyltransferase was isolated by histone-Sepharose affinity chromatography from human cord blood red cells. The enzyme was detected only in very young red cells. The semipurified enzyme and [14C]acetyl-CoA were used to acetylate isolated Hb F tetramer and alpha and gamma subunits. The in vitro acetylated products were characterized by globin chain separation by CM-cellulose chromatography and tryptic peptide analysis by reverse-phase HPLC. Acetylation of both the gamma-chains and the alpha-chains could occur within the Hb F tetramer. Acetylation also could take place on intact subunits. It appears that some Hb FIC could be formed in the cells by utilizing Hb F or free gamma-chains as acetylation substrate.
authors.affiliation: Department of Cell and Molecular Biology, Medical College of Georgia, Augusta 30912-2100.
authors.forename: C C
authors.initials: CC
authors.lastname: Qiu
authors.forename: J
authors.initials: J
authors.lastname: Kasten-Jolly
authors.forename: E C
authors.initials: EC
authors.lastname: Abraham
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000097:blood*; D002846:Chromatography, Affinity; D004912:Erythrocytes / Q000201:enzymology*; D006454:Hemoglobins / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism
chemical_list: D006454:Hemoglobins; D006657:Histones; D011506:Proteins; D000123:Acetyltransferases