Russell W C, Blair G E
J Gen Virol. 1977 Jan;34(1):19-35. doi: 10.1099/0022-1317-34-1-19.
Cells infected with human adenovirus type 5 have been labelled with 32P-orthophosphate under various conditions and extracts examined, after denaturation in sodium dodecyl sulphate (SDS), by polyacrylamide gel electrophoresis (PAGE) followed by autoradiography. A number of polypeptides appear to be phosphorylated specifically as a result of infection. Early in infection, phosphorylation of a polypeptide of apparent mol. wt. 26 K associated with ribosomes can be detected. Two other phosphorylated polypeptides of apparent mol. wt. 72 K and 18 K can also be seen, the former being mainly confined to the nucleus and capable of being precipitated by the previously described virus-specific P antiserum. The 18 K phosphorylated polypeptide is found mainly in association with membrane fractions. Later in infection phosphorylated polypeptides of apparent mol. wt. 100 K and 39 K can be recognized, the former being associated with ribosomes but removed, however, with a high salt wash; the latter component is mainly detected in the nucleus. Analysis of the purified 32P-labelled virus by the SDS PAGE technique indicated that a structural polypeptide of apparent mol. wt. 66 K (IIIa) was also phosphorylated.
在不同条件下，用32P - 正磷酸盐标记感染了5型人类腺病毒的细胞，并在十二烷基硫酸钠（SDS）中变性后，通过聚丙烯酰胺凝胶电泳（PAGE）和放射自显影检查提取物。许多多肽似乎因感染而被特异性磷酸化。在感染早期，可以检测到与核糖体相关的表观分子量为26K的多肽发生磷酸化。还可以看到另外两种表观分子量为72K和18K的磷酸化多肽，前者主要局限于细胞核，并且能够被先前描述的病毒特异性P抗血清沉淀。18K磷酸化多肽主要与膜部分相关。在感染后期，可以识别表观分子量为100K和39K的磷酸化多肽，前者与核糖体相关，但用高盐洗涤后会被去除；后者主要在细胞核中检测到。通过SDS - PAGE技术对纯化的32P标记病毒进行分析表明，表观分子量为66K的结构多肽（IIIa）也被磷酸化。
