Published 1988
| Version v1
Journal article
Human red cell acetyltransferase
Description
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 α and γ 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 γ-chains and the α-chains could occur within the Hb F tetramer. Acetylation also could take place on intact subunits. It appears that some Hb F/sub Ic/ could be formed in the cells by utilizing Hb F or free γ-chains as acetylation substrate
Additional details
Publishing Information
- Journal Title
- Life Sci.
- Journal Volume
- 42
- Journal Issue
- 26
- Series
- Life Sci.
- Journal Page Range
- 2739-2748
- ISSN
- 0024-3205
- CODEN
- LIFSA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 19088388
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- ACETYLATION; CARBON 14 COMPOUNDS; ERYTHROCYTES; LIQUID COLUMN CHROMATOGRAPHY; MAN; TRACER TECHNIQUES; TRANSFERASES
- Descriptors DEC
- ACYLATION; ANIMALS; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CARBON COMPOUNDS; CHEMICAL REACTIONS; CHROMATOGRAPHY; ENZYMES; ISOTOPE APPLICATIONS; MAMMALS; MATERIALS; ORGANIC COMPOUNDS; PRIMATES; SEPARATION PROCESSES; VERTEBRATES