Pig Liver Translational Initiation Factor eIF-2. N-Terminal Amino Acid Sequences of α and γ Subunits and the Phosphorylation Site Stucture(Biological Chemistry)

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Eukaryotic initiation factor eIF-2 has key roles in the initiation of protein synthesis. This work describes a partial characterization of pig liver eIF-2 and the phosphorylation site sequence of the a subunit. Our pig liver eIF-2 was composed of a and y subunits. The N-terminal sequences of these subunits were analyzed by an automated Edman degradation. Forty residues of the N-terminal sequences of the a subunit were identified; they were mostly hydrophobic amino acids. On the other hand, we identified only 19 residues of the N-terminal sequence of the j subunit, since pig liver eIF-2γ contained a minor component having a sequence lacking the N-terminal Ala-Gly of the γ subunit. Exhaustive tryptic digestion of [^<32>P]-and [^3H]carboxymethyl-labeled eIF_γ2α produced one major phosphopeptide. The peptide was purified by one dimensional thin-layer chromatography and high performance liquid chromatography. The sequence of the peptide was Ser-Glu-Leu-Ser(P)-Arg-Arg.
社団法人日本農芸化学会の論文
1988-06-23