Norrild B, Andersen A B, Feldborg R
Arch Virol. 1985;85(1-2):95-108. doi: 10.1007/BF01317009.
Herpes simplex virus type 2 proteins extracted from infected cells and analysed by crossed immunoelectrophoresis identified a nonglycosylated antigen named Ag-5. The antigen contained two proteins when extracted from the agarose gel and the molecular weights were 128K and 91K. Both proteins are located in the nucleus of the infected cells and the 128K is identical to ICP-8. The 91K protein is based on the reactivity with monoclonal antibodies most likely the alkaline exonuclease mapped by Preston and Cordingly (25). Our data show that although the proteins ICP-8 and 91K coprecipitate they differ in both peptide composition and in immunological specificity.
从感染细胞中提取并通过交叉免疫电泳分析的单纯疱疹病毒2型蛋白鉴定出一种名为Ag-5的非糖基化抗原。当从琼脂糖凝胶中提取时,该抗原包含两种蛋白质,分子量分别为128K和91K。这两种蛋白质都位于感染细胞的细胞核中,128K的蛋白质与ICP-8相同。91K蛋白质基于与单克隆抗体的反应性,很可能是由普雷斯顿和科丁利(25)定位的碱性核酸外切酶。我们的数据表明,尽管ICP-8和91K蛋白能共沉淀,但它们在肽组成和免疫特异性上都有所不同。