Erikson R L, Collett M S, Erikson E, Purchio A F, Brugge J S
Prog Clin Biol Res. 1980;41:747-56.
The product of the avian sarcoma virus (ASV) transforming gene is a 60,000-dalton phosphoprotein, pp60src. Sera from mice and from an occasional rabbit bearing ASV-induced tumors are capable of immunoprecipitating a phosphoprotein of similar, but not identical, structure from normal avian and mammalian cells. This protein is presumed to be the product of the cellular sarc gene, and has been tentatively designated pp60sarc. Analysis of the tryptic phosphopeptides reveals that the viral and avian proteins have an apparently identical phosphoserine-containing peptide. They evidently also both have an analogous phosphothreonine residue surrounded by a different amino acid sequence. Immunoprecipitates containing either the viral or normal cellular pp60 protein catalyze the transfer of radiolabeled phosphate from [gamma-32P]-ATP to the heavy chain of immune rabbit IgG, therefore suggesting that both viral and cellular phosphoproteins may be protein kinases.
禽肉瘤病毒(ASV)转化基因的产物是一种60,000道尔顿的磷蛋白,即pp60src。来自患有ASV诱导肿瘤的小鼠以及偶尔的兔子的血清,能够从正常禽类和哺乳动物细胞中免疫沉淀出结构相似但不完全相同的磷蛋白。这种蛋白质被推测为细胞sarc基因的产物,并被暂定命名为pp60sarc。对胰蛋白酶磷酸肽的分析表明,病毒蛋白和禽类蛋白具有一个明显相同的含磷酸丝氨酸的肽段。它们显然还都有一个被不同氨基酸序列包围的类似磷酸苏氨酸残基。含有病毒或正常细胞pp60蛋白的免疫沉淀物催化放射性标记的磷酸从[γ-32P]-ATP转移到免疫兔IgG的重链上,因此表明病毒和细胞磷蛋白可能都是蛋白激酶。