Moore R E, Sharma R K
Endocrinology. 1980 Oct;107(4):1264-5. doi: 10.1210/endo-107-4-1264.
Free and membrane-bound polysomes were isolated and incubated under in vitro conditions that allowed the phosphorylation of contained poly(A)mRNP complexes. The three phosphoproteins of 150,000, 67,000 and 45,000 daltons were consistently present in the free poly(A)mRNP fraction and absent in the membrane-bound particles. The major phosphoprotein contained in the membrane-bound poly(A)mRNP complexes was 105,000 daltons. This protein was also present in the free cytoplasmic poly(A)mRNP fraction. It is conceivable that protein kinases differentially regulate these two classes of poly(A)mRNP particles through specific phosphorylations of their associated proteins.
分离出游离的和膜结合的多核糖体,并在体外条件下进行孵育,该条件允许所含的聚腺苷酸(poly(A))信使核糖核蛋白(mRNP)复合物发生磷酸化。150,000、67,000和45,000道尔顿的三种磷蛋白始终存在于游离的聚腺苷酸信使核糖核蛋白组分中,而不存在于膜结合颗粒中。膜结合的聚腺苷酸信使核糖核蛋白复合物中所含的主要磷蛋白为105,000道尔顿。这种蛋白质也存在于游离的细胞质聚腺苷酸信使核糖核蛋白组分中。可以想象,蛋白激酶通过对其相关蛋白质的特异性磷酸化来差异调节这两类聚腺苷酸信使核糖核蛋白颗粒。