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- W342555093 abstract "ABSTRACT The molecular structure of eIF-2 has been determined to be an αβγ trimer of molecular weight 122,000. The GTP initially bound by eIF-2 to form a soluble ternary complex appears to be the same GTP that is hydrolyzed as a prerequisite for subunit joining. Using the above information, experiments were performed to test the effect of HCR mediated phosphorylation of eIF-2 on the biologic function of eIF-2. In every assay tested, whether rate or extent of reaction was measured, there appeared to be no difference in biologic activity between phosphorylated and non-phosphorylated eIF-2." @default.
- W342555093 created "2016-06-24" @default.
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- W342555093 date "1979-01-01" @default.
- W342555093 modified "2023-09-27" @default.
- W342555093 title "EFFECT OF PHOSPHORYLATION ON eIF-2" @default.
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- W342555093 doi "https://doi.org/10.1016/b978-0-12-066250-0.50028-4" @default.
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