Cross R K, Fields B N
J Virol. 1976 Jul;19(1):162-73. doi: 10.1128/JVI.19.1.162-173.1976.
The electrophoretic analysis of reovirus-specific polypeptides in infected cells using a discontinuous gel system has allowed the resolution of additional viral-specific polypeptides, including one large-sized gamma3 and two (or possibly three) medium-sized (mu3, mu4, mu5(?)) species. The proteins designated mu0, sigma1, and sigma2 based on electrophoretic mobility in gel systems containing phosphate-urea correspond to mu4, sigma2, and sigma1, respectively, when analyzed in systems containing Tris-glycine. It is likely that protein modifications (phosphorylation and glycosylation) are responsible for at least some of these differences.
使用不连续凝胶系统对感染细胞中呼肠孤病毒特异性多肽进行电泳分析,已分辨出其他病毒特异性多肽,包括一种大尺寸的γ3和两种(或可能三种)中等尺寸的(μ3、μ4、μ5(?))种类。在含有磷酸盐-尿素的凝胶系统中根据电泳迁移率命名的蛋白质μ0、σ1和σ2,在含有Tris-甘氨酸的系统中分析时,分别对应于μ4、σ2和σ1。蛋白质修饰(磷酸化和糖基化)可能至少是造成其中一些差异的原因。