Gander E S, Mueller R U, Goldenberg S, Morel C
Mol Biol Rep. 1975 Dec;2(4):343-9. doi: 10.1007/BF00357022.
Duck- and rabbit globin messenger ribonucleoprotein complexes isolated by oligo(dT) cellulose chromatography reveal an identical protein pattern-two main proteins of molecular weights of 73,000 and 49,000 daltons and minor components-whether the complexes have been liberated from polyribosomes with the EDTA- or the puromycin-high-salt method. In the globin messenger ribonucleoprotein particles of both species predominantly the protein with a molecular weight of 73,000 daltons is attached to poly(A)-containing regions of the messenger RNAs.
通过寡聚(dT)纤维素色谱法分离得到的鸭和兔珠蛋白信使核糖核蛋白复合物,无论其是用EDTA法还是嘌呤霉素-高盐法从多核糖体中释放出来的,都呈现出相同的蛋白质模式——两种主要蛋白质,分子量分别为73,000和49,000道尔顿,以及一些次要成分。在这两个物种的珠蛋白信使核糖核蛋白颗粒中,分子量为73,000道尔顿的蛋白质主要附着于信使核糖核酸的含多聚(A)区域。