Davis J, Gilden R V, Oroszlan S
Intervirology. 1975;5(1-2):21-30. doi: 10.1159/000149877.
Limited tryptic digestion of p30 antigen (the major internal viral protein) of type C viruses isolated from hamster, rat, and gibbon ape yielded a polypeptide fragment with a molecular weight of approximately 10,000 daltons. Some antigenic determinants with interspecies specificity were retained on these polypeptides, which in serological tests cross-reacted with antibody produced previously against a similar fragment obtained from mouse p30. Exhaustive trypsinization resulted in further fragmentation with concomitant loss of serologic activity. The results suggest that all mammalian type C virus p30s have an antigenically related polypeptide core which is not readily digested by trypsin.
对从仓鼠、大鼠和长臂猿中分离出的C型病毒的p30抗原(主要的病毒内部蛋白)进行有限的胰蛋白酶消化,产生了一个分子量约为10,000道尔顿的多肽片段。这些多肽上保留了一些具有种间特异性的抗原决定簇,在血清学检测中,它们与先前针对从小鼠p30获得的类似片段产生的抗体发生交叉反应。彻底的胰蛋白酶消化导致进一步的片段化,并伴随着血清学活性的丧失。结果表明,所有哺乳动物C型病毒的p30都有一个抗原相关的多肽核心,不易被胰蛋白酶消化。