Farrar G H, Greenaway P J
J Gen Virol. 1986 Jul;67 ( Pt 7):1469-73. doi: 10.1099/0022-1317-67-7-1469.
Three disulphide cross-bridged glycoprotein complexes were immunoprecipitated from purified human cytomegalovirus envelopes using a monoclonal antibody with a specificity for a glycoprotein of mol. wt. 52 X 10(3). These complexes were isolated by electroelution after polyacrylamide gel electrophoresis (PAGE) under non-reducing conditions. Compositional analysis of each complex by PAGE under reducing conditions showed that at least two distinct complexes, one containing glycoproteins with mol. wt. of 52 X 10(3) and 95 X 10(3) and the other with glycoproteins of 52 X 10(3) and 130 X 10(3), were present. The results obtained indicated that one of these complexes could also exist as a dimer.
使用对分子量为52×10³的糖蛋白具有特异性的单克隆抗体，从纯化的人巨细胞病毒包膜中免疫沉淀出三种二硫键交联的糖蛋白复合物。这些复合物在非还原条件下进行聚丙烯酰胺凝胶电泳（PAGE）后通过电洗脱分离。在还原条件下通过PAGE对每个复合物进行组成分析表明，存在至少两种不同的复合物，一种含有分子量为52×10³和95×10³的糖蛋白，另一种含有分子量为52×10³和130×10³的糖蛋白。所得结果表明，这些复合物中的一种也可以以二聚体形式存在。
