Suh M
J Virol. 1982 Mar;41(3):1095-8. doi: 10.1128/JVI.41.3.1095-1098.1982.
Transformation of hamster embryo cells by herpes simplex virus stimulated the production of a 35-kilodalton (35K) protein that was specifically immunoprecipitated, along with other polypeptides, by rabbit hyperimmune serum. This 35K polypeptide was further analyzed by partial digestion with Staphylococcus aureus V8 protease in parallel with a 35K polypeptide from herpes simplex virus type 2-infected cells. These polypeptides had almost identical partial-proteolytic cleavage maps, indicating that they are probably the same or that they are very similar polypeptides.
单纯疱疹病毒对仓鼠胚胎细胞的转化刺激了一种35千道尔顿(35K)蛋白质的产生,该蛋白质与其他多肽一起被兔超免疫血清特异性免疫沉淀。用金黄色葡萄球菌V8蛋白酶部分消化该35K多肽,并与来自2型单纯疱疹病毒感染细胞的35K多肽进行平行分析。这些多肽具有几乎相同的部分蛋白水解裂解图谱,表明它们可能是相同的或非常相似的多肽。