Protein Synthesis in Rabbit Reticulocytes
نویسندگان
چکیده
منابع مشابه
Factors affecting protein synthesis in vitro in rabbit reticulocytes.
Rabbit reticulocytes in vitro rapidly incorporate labeled amino acids into their proteins. The process is accelerated by the plasma of every mammal investigated and also by extracts of normal erythrocytes, rabbit reticulocytes, liver, spleen, and yeast (1). We have described two sets of stimulating factors: one of these sets consists of certain amino acids (I), the other of fructose-amino acids...
متن کاملProtein synthesis in rabbit reticulocytes: Characteristics of a ribosomal factor that reverses inhibition of protein synthesis
A ribosomal salt (0.5 M KCI) wash factor (RF) that reverses inhibition of protein synthesis in heme-deficient reticulocyte lysates has been resolved from the bulk of MettRNAfmet-binding factor (EIF-1), Co-EIF-I, and EIF-2 (ternary complex dissociation factor, TDF). The purified RF restores protein synthesis activity of heme-deficient lysates to the level observed in the presence of hemin. No di...
متن کاملProtein synthesis in rabbit reticulocytes: mechanism of protein synthesis inhibition by heme-regulated inhibitor.
Partially purified Met-tRNAf binding factor, eIF-2, was phosphorylated by using heme-regulated inhibitor (HRI). Phosphorylated eIF-2 was freed from HRI by phosphocellulose column chromatography. Analysis by isoelectric focusing showed 100% phosphorylation of the 38,000-dalton subunit of eIF-2. Both eIF-2 and eIF-2(P) formed ternary complexes with Met-tRNAf and GTP with almost the same efficienc...
متن کاملProtein synthesis in rabbit reticulocytes: characteristics of CO-eIF-2 protein complex.
A high molecular weight reticulocyte protein factor, named Co-eIF-2, contains Co-eIF-2A, Co-eIF-2B, and Co-eIF-2C activities and stimulates Met-tRNAf binding to eIF-2 both in the presence and absence of Mg2+. Some characteristics of this stimulation in the absence of Mg2+ are: (1) Stimulation is most pronounced at low eIF-2 levels. (2) Stimulation is partially resistant to heat and NEM treatmen...
متن کاملProtein synthesis in rabbit reticulocytes. Preparation of homogeneous Met-tRNAf deacylase and studies of its role in protein synthesis.
Met-tRNAf deacylase from reticulocyte ribosomes has been purified to homogeneity. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the homogeneous preparation gives a single protein band corresponding to a molecular weight of approximately 67,000. Purified Met-tRNAf deacylase degrades free Met-tRNAf and also Met-tRNAf bound to 40 S ribosomes in the presence of AUG codon but does ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43794-0