Snyder H W, Singhal M C
Cancer Invest. 1983;1(3):225-36. doi: 10.3109/07357908309041362.
The translation products of the Snyder-Theilen (ST) and Gardner-Arnstein (GA) strains of feline sarcoma virus (FeSV), termed gag-fes proteins, are high molecular weight polyproteins containing different amounts of the amino terminus of the feline leukemia virus (FeLV) gag gene-coded precursor protein linked to a similar sarcoma virus-specific polypeptide. Both polyproteins are phosphoproteins with indistinguishable in vitro associated tyrosine-specific protein kinase activities. The polyproteins are extremely hydrophobic proteins which are intimately associated with the plasma membrane fraction of transformed cells. Approximately 10% of the proteins are modified by glycosylation and expressed on the cell surface where they are accessible to lactoperoxidase-mediated radio-iodination and trypsinization. Cell surface localization of the polyproteins does not appear to be necessary for transformation. However, preliminary evidence suggests that the amount of FeLV p30 sequences at the amino end of the proteins may have some effect on the intracellular distribution of the gag-fes polyproteins and on the phenotype of the transformed cell.
猫肉瘤病毒（FeSV）的斯奈德 - 泰伦（ST）株和加德纳 - 阿恩斯坦（GA）株的翻译产物，即gag - fes蛋白，是高分子量多聚蛋白，包含不同量的与类似肉瘤病毒特异性多肽相连的猫白血病病毒（FeLV）gag基因编码前体蛋白的氨基末端。这两种多聚蛋白都是磷蛋白，具有难以区分的体外相关酪氨酸特异性蛋白激酶活性。这些多聚蛋白是极具疏水性的蛋白，与转化细胞的质膜部分紧密相关。约10%的蛋白通过糖基化修饰并在细胞表面表达，在那里它们可被乳过氧化物酶介导的放射性碘化和胰蛋白酶消化作用所作用。多聚蛋白的细胞表面定位对于转化似乎并非必要。然而，初步证据表明，蛋白氨基末端的FeLV p30序列的量可能对gag - fes多聚蛋白的细胞内分布以及转化细胞的表型有一定影响。
