Human red cell acetyltransferase.
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.
Qiu
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CC
Department of Cell and Molecular Biology, Medical College of Georgia, Augusta 30912-2100.
Kasten-Jolly
J
J
Abraham
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EC
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
D006454:Hemoglobins; D006657:Histones; D011506:Proteins; D000123:Acetyltransferases