Document Detail


Human fetal hemoglobin synthesis and its NH2-terminal acetylation in a rabbit reticulocyte lysate translational system.
MedLine Citation:
PMID:  2420364     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The biosynthesis of the acetylated (Hb FIc) and the non-acetylated (Hb F0) human fetal hemoglobin components has been examined in a cell-free translational system. The poly(A)-RNA was isolated from umbilical cord blood samples and translated in the heterologous translational system derived from rabbit reticulocyte lysates in the presence of labeled amino acid(s) or acetyl-CoA. The amount of each hemoglobin or globin chain made in the system was determined by separating the synthesis products by cation-exchange chromatographic methods. The in vitro synthesis ratios were close to the FIc/Ftotal values of the respective hemolysates. The same conclusion could be reached by determining the specific activity ratios of Hb FIc/Hb F0. Co-migration of radioactivity peaks with absorbance peaks indicated the synthesis of that hemoglobin or globin chain. Confirmation of the synthesis of true gamma 0 and gamma Ic was accomplished by high-pressure liquid chromatographic separation of 3H-labeled tryptic peptides. Each peptide corresponded well with the radioactivity peak. Labeled acetyl-group incorporation into Hb FIc and gamma IcT-1 provided direct evidence for acetylation of gamma chains in Hb FIc. The data indicate that the mRNA itself dictates whether a protein is acetylated and, if so, to what extent. The control appears to be not unique to the human red cell system.
Authors:
J Kasten-Jolly; E C Abraham
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  866     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1986 Mar 
Date Detail:
Created Date:  1986-04-29     Completed Date:  1986-04-29     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  125-34     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acetylation
Acetyltransferases / metabolism
Animals
Cell-Free System
Chromatography, High Pressure Liquid
Fetal Hemoglobin / analogs & derivatives*,  biosynthesis
Humans
Poly A / metabolism
Protein Biosynthesis
Protein Processing, Post-Translational
RNA, Messenger / metabolism
Rabbits
Reticulocytes / metabolism*
Grant Support
ID/Acronym/Agency:
AM-32957/AM/NIADDK NIH HHS; HL-29554/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/RNA, Messenger; 0/acetylated human fetal hemoglobin; 24937-83-5/Poly A; 9034-63-3/Fetal Hemoglobin; EC 2.3.1.-/Acetyltransferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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