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Human red cell acetyltransferase.

C C Qiu1, J Kasten-Jolly, E C Abraham

  • 1Department of Cell and Molecular Biology, Medical College of Georgia, Augusta 30912-2100.

Life Sciences
|January 1, 1988
PubMed
Summary
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Human cord blood red cells contain acetyltransferase, an enzyme that acetylates hemoglobin F (Hb F) and its subunits. This process, observed in young red cells, may form Hb FIC in vivo.

Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Hemoglobin F (Hb F) is the primary non-adult hemoglobin.
  • Red blood cells undergo various post-translational modifications.

Purpose of the Study:

  • To investigate the presence and activity of acetyltransferase in human red blood cells.
  • To characterize the in vitro acetylation of Hb F and its subunits.

Main Methods:

  • Isolation of acetyltransferase using histone-Sepharose affinity chromatography.
  • In vitro acetylation of Hb F tetramer and isolated alpha and gamma subunits using [14C]acetyl-CoA.
  • Characterization of acetylated products via CM-cellulose chromatography and reverse-phase HPLC.

Main Results:

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  • Acetyltransferase was detected exclusively in very young human cord blood red cells.
  • Both gamma-chains and alpha-chains of Hb F can be acetylated in vitro, either within the tetramer or as intact subunits.
  • The study suggests potential in vivo formation of Hb FIC from Hb F or free gamma-chains.

Conclusions:

  • Human red blood cells possess acetyltransferase activity capable of modifying hemoglobin.
  • Acetylation of hemoglobin subunits occurs in vitro, indicating potential regulatory mechanisms in red cell development.