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Acetyltransferase and human hemoglobin acetylation

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5333028
A minor component of human fetal hemoglobin (Hb F) is acetylated at the amino-terminus of the ..gamma..-globin chains. A similar minor component of Hb F is formed during translation of cord blood mRNA in the rabbit reticulocyte lysate system. The acetylation appeared to be enzymatic. This system contains an acetyltransferase capable of acetylating histones and hemoglobins. The enzyme, partially purified by histone-Sepharose affinity chromatography was capable of incorporating labeled acetyl- group from 1-(/sup 14/C-acetyl)-CoA into both human Hb F/sub 0/ and HB A/sub 0/, but at a lower rate than for histones. Characterization of the labeled products indicated that the ..cap alpha..-chains of both hemoglobins were being acetylated presumably at a lysyl-residue, but in the case of Hb F/sub 0/ the amino-terminus of the ..gamma..-globin chains was acetylated as well. While histone-Sepharose bound more than 95% of the enzyme, Sepharose linked Hb F/sub 0/, ..gamma..-globin chains, and Hb Bart's bound 14, 5, and 12% of the activity, respectively. Enzyme bound to these resins was not any more active on the hemoglobins than was the enzyme bound to the histone-Sepharose. The histone-Sepharose was also used to detect the enzyme in human cord blood red cells separated by dextran 40 density gradient centrifugation. Activity was found mostly in the young cells, and was directly related to the number of reticulocytes present in any one fraction.
Research Organization:
Medical College of Georgia, Augusta
OSTI ID:
5333028
Report Number(s):
CONF-8606151-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:6
Country of Publication:
United States
Language:
English