Abstract
Ternary complex formation between [3H]Met-tRNAf, [14C]H3-eIF-2, and GTP was measured on nitrocellulose filters. It is shown that [3H]Met-tRNAf and [14C]H3-eIF-2 are present on the filter in equimolar amounts when ATP, creatine phosphate, and creatine kinase are included in the reaction mixture. Under these conditions the factor is 100% active. With small amounts of factor significant losses occur due to adsorption to the wall of the reaction vessels, resulting in seemingly low activities of eIF-2. These losses can be prevented by the presence of "stimulatory" proteins, which enhance the recovery of both [3H]Met-tRNAf and [14C]H3-eIF-2 on the filter but do not alter their ratio.
Highlights
Protein fraction that gave a 2-fold stimulation of ternary complex formation at low concentrations of eIF-2 (less than 2 pmol/25 ~1 of reaction mixture) was isolated from rabbit reticulocyte lysate and fractionated on columns of Sepharose-heparin
From the Department of Molecular Cell Biology, University and Harry 0
We show that some proteins isolated from the lysate of rabbit reticulocytes enhance the amounts of eIF-2 recovered on the filter and, in doing so, seemingly stimulate ternary complex formation
Summary
Protein fraction that gave a 2-fold stimulation of ternary complex formation at low concentrations of eIF-2 (less than 2 pmol/25 ~1 of reaction mixture) was isolated from rabbit reticulocyte lysate and fractionated on columns of Sepharose-heparin When GDP is incubated with creatine phosphate and creatine kinase prior to its addition to eIF-2 and Met-tRNAr, it can be utilized for ternary complex formation (Table I).
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