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Human red cell acetyltransferase.

C C Qiu·J Kasten-Jolly·E C Abraham
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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.

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AcetylationAcetyltransferasesChromatography, AffinityErythrocytesHemoglobinsHistonesHumansProtein BindingProteinsJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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C C Qiu, J Kasten-Jolly, E C Abraham. 1988. Human red cell acetyltransferase.. https://doi.org/10.1016/0024-3205(88)90251-2

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