Todorov I T, Noll F, Hadjiolov A A
Eur J Biochem. 1983 Mar 15;131(2):271-5. doi: 10.1111/j.1432-1033.1983.tb07259.x.
Nucleolar '80-S' and '40-S' preribosomes (containing 45-S and 21-S pre-rRNA, respectively), as well as cytoplasmic ribosomes, were isolated from Friend erythroleukemia cells. The presence of structural ribosomal proteins in the isolated particles was studied by using antisera against individual rat liver small ribosomal subunit proteins. The analysis is based on the established crossreactivity between rat and mouse ribosomes [F. Noll and H. Bielka (1970) Mol. Gen. Genet. 106, 106-113]. The identification of the proteins was achieved by two independent immunological techniques: the passive haemagglutination test and the enzyme immunoassay of electrophoretically fractionated proteins, blotted on nitrocellulose. All 17 proteins tested are present in cytoplasmic ribosomes. A large number of proteins (S3a, S6, S7, S8, S11, S14, S18, S20, S23/24 and S25) are present in the '80-S' preribosome. Only two proteins (S3 and S21) are added during the formation of the '40-S' preribosome in the nucleolus. Four proteins (S2, S19, S26 and S29) are added at later, possibly extranucleolar, stages of ribosome formation. The results obtained provide evidence for the sequential addition of proteins during the formation of the small ribosomal subunit in Friend erythroleukemia cells.
从弗氏红白血病细胞中分离出核仁“80 - S”和“40 - S”前核糖体（分别含有45 - S和21 - S前体rRNA）以及细胞质核糖体。利用针对大鼠肝脏小核糖体亚基蛋白质的抗血清研究了分离颗粒中核糖体结构蛋白的存在情况。该分析基于已确定的大鼠和小鼠核糖体之间的交叉反应性[F.诺尔和H.比尔卡（1970年）《分子遗传学与普通遗传学》106卷，第106 - 113页]。通过两种独立的免疫技术实现了蛋白质的鉴定：被动血凝试验和对电泳分离后印迹在硝酸纤维素膜上的蛋白质进行酶免疫测定。所检测的全部17种蛋白质都存在于细胞质核糖体中。大量蛋白质（S3a、S6、S7、S8、S11、S14、S18、S20、S23/24和S25）存在于“80 - S”前核糖体中。在核仁中“40 - S”前核糖体形成过程中仅添加了两种蛋白质（S3和S21）。四种蛋白质（S2、S19、S26和S29）在核糖体形成的后期、可能是核仁外阶段添加。所获得的结果为弗氏红白血病细胞中小核糖体亚基形成过程中蛋白质的顺序添加提供了证据。
