Abstract
Two nonerythropoietic tissues, brian and liver, contain an initiation factor that can overcome the block in initiation of protein synthesis seen in reticulocyte lysates when exogenous hemin is not present. Upon incubation of the brain factor with hemin and removal of free hemin by gel filtration, the factor activity is strongly stimulated. This stimulation shows a concentration dependence on hemin close to that seen for stimulation of protein synthesis in whole reticulocyte lysates. The data indicate that hemin mediates the formation of an active initiation factor complex from inactive, lower molecular weight components.
MeSH Terms
Animals
Brain Chemistry
Cell-Free System
Chromatography, Gel
Heme/pharmacology,physiology
Kinetics
Liver/analysis
Mice
Peptide Initiation Factors/isolation & purification
Polyribosomes/metabolism
Protein Biosynthesis
Rabbits
Rats
Reticulocytes/metabolism,ultrastructure
Stimulation, Chemical
Chemicals
Peptide Initiation Factors
Heme
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Raffel C
Stein S
Kaempfer R
References (10)
10 references, click to expand
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