Pulikowska J, Twardowski T
Acta Biochim Pol. 1982;29(3-4):245-58.
Three forms of elongation factor 1 (EF1A, EF1B and EF1C) were isolated from wheat germ; the preparation obtained by successive chromatography on DEAE-Sephadex A-50, hydroxylapatite and Sephadex G-200 showed about 90% purity. The molecular masses of these forms were about: 61 000, 48 000 and 12 500, respectively. EF1A was the only form which formed the ternary complex GTP-EF1-AA-tRNA and was the most active in binding of Phe-tRNA to the poly-U programmed ribosomes. Based on the data of amino acid analysis, N-terminal amino acid determination and previously described proteolysis (Pulikowska et al., Biochem. Biophys. Res. Commun., 1979, 91, 1011-1017), it is assumed that EF1C is a basic structural subunit of elongation factor EF1 from wheat germ, but only EF1A shows the conformation-dependent full biological activity.
从小麦胚芽中分离出了三种延伸因子1（EF1A、EF1B和EF1C）；通过先后在DEAE-葡聚糖A-50、羟基磷灰石和葡聚糖G-200上进行层析得到的制剂显示纯度约为90%。这些形式的分子量分别约为：61000、48000和12500。EF1A是唯一能形成三元复合物GTP-EF1-AA-tRNA的形式，并且在将苯丙氨酰-tRNA结合到聚-U编程核糖体上时活性最高。根据氨基酸分析、N端氨基酸测定以及先前描述的蛋白水解数据（Pulikowska等人，《生物化学与生物物理研究通讯》，1979年，91卷，1011 - 1017页），推测EF1C是小麦胚芽延伸因子EF1的基本结构亚基，但只有EF1A表现出构象依赖性的完全生物学活性。
