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.
journal_name
Life Scijournal_title
Life sciencesauthors
Qiu CC,Kasten-Jolly J,Abraham ECdoi
10.1016/0024-3205(88)90251-2subject
Has Abstractpub_date
1988-01-01 00:00:00pages
2739-48issue
26eissn
0024-3205issn
1879-0631pii
0024-3205(88)90251-2journal_volume
42pub_type
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