Suzuki H, Kishio N, Morozumi K, Ichimori K, Mukouyama E B
J Biochem. 1985 Apr;97(4):1061-6. doi: 10.1093/oxfordjournals.jbchem.a135148.
The specific phosphorylation of pig liver initiation factor 2(eIF-2) by the N-ethylmaleimide (NEM)-treated hemin-controlled translational inhibitor (HCI) from rabbit reticulocytes was investigated. The inhibitor phosphorylated the serine residue of the alpha subunit of eIF-2 (eIF-2 alpha) and 1 mol of phosphate was incorporated into 1 mol of eIF-2 alpha by the inhibitor on maximal phosphorylation, even when eIF-2 was pretreated with alkaline phosphatase prior to phosphorylation. The 32P-labeled eIF-2 alpha was subjected to tryptic digestion and the tryptic digest was analyzed by two-dimensional peptide mapping on a cellulose thin-layer sheet. After 94 h digestion, the autoradiograph of the peptide map showed a single 32P-labeled band with a molecular weight of approximately 1,200. These findings suggest that one specific serine residue of pig liver eIF-2 alpha was phosphorylated by the NEM-treated HCI.
研究了经N-乙基马来酰亚胺（NEM）处理的来自兔网织红细胞的血红素控制的翻译抑制剂（HCI）对猪肝起始因子2（eIF-2）的特异性磷酸化作用。该抑制剂使eIF-2的α亚基（eIF-2α）的丝氨酸残基磷酸化，在最大磷酸化时，1摩尔的磷酸被掺入1摩尔的eIF-2α中，即使在磷酸化之前用碱性磷酸酶预处理eIF-2也是如此。将32P标记的eIF-2α进行胰蛋白酶消化，并在纤维素薄层板上通过二维肽图谱分析胰蛋白酶消化产物。消化94小时后，肽图谱的放射自显影片显示出一条分子量约为1200的单一32P标记带。这些发现表明，经NEM处理的HCI使猪肝eIF-2α的一个特定丝氨酸残基磷酸化。
