Heilman C J, Zweig M, Hampar B
J Virol. 1981 Nov;40(2):508-15. doi: 10.1128/JVI.40.2.508-515.1981.
Intracellular p40 is a class of protein ranging in molecular weight from 39,000 to 45,000 that is immunoprecipitated from herpes simplex virus type 1 (HSV-1)- and HSV-2-infected cell extracts by mouse monoclonal antibodies or guinea pig antisera against HSV-1 and HSV-2 nucleocapsid p40. Analysis by a two-dimensional gel system showed that HSV-1 and HSV-2 intracellular p40 each consisted of three major components. However, these HSV-1 and HSV-2 proteins differed in charge and size. Analysis of Staphylococcus aureus V8 protease partial digests by two-dimensional gel electrophoresis indicated that none of the peptides of HSV-1 and HSV-2 intracellular p40 were identical. Immunoprecipitation of the partial digest products of intracellular p40-1 and p40-2 with homologous and heterologous guinea pig antisera resulted in the precipitation of various combinations of peptides indicating the presence of either type-specific or cross-reactive antigenic determinants.
细胞内p40是一类分子量在39,000至45,000之间的蛋白质,可通过小鼠单克隆抗体或针对单纯疱疹病毒1型(HSV-1)和HSV-2核衣壳p40的豚鼠抗血清,从感染HSV-1和HSV-2的细胞提取物中免疫沉淀得到。二维凝胶系统分析表明,HSV-1和HSV-2的细胞内p40各自均由三个主要成分组成。然而,这些HSV-1和HSV-2蛋白在电荷和大小上有所不同。通过二维凝胶电泳对金黄色葡萄球菌V8蛋白酶部分消化产物的分析表明,HSV-1和HSV-2细胞内p40的肽段均不相同。用同源和异源豚鼠抗血清对细胞内p40-1和p40-2的部分消化产物进行免疫沉淀,导致各种肽段组合的沉淀,表明存在型特异性或交叉反应性抗原决定簇。