在平板凝胶中分离的黄病毒蛋白之间的异质性。

Heterogeneity among flavivirus proteins separated in slab gels.

作者信息

Westaway E G, McKimm J L, McLeod L G

出版信息

Arch Virol. 1977;53(4):305-12. doi: 10.1007/BF01315629.

Abstract

35S-methionine-labeled proteins specified in Vero cells by flaviviruses were analysed by SDS-phosphate electrophoresis in polyacrylamide slab gels. The clarity of the profile produced by Kunjin virus permitted designation of the nonstructural proteins, and confirmed the identity of NV21/2; the profile included a protein previously designated V2 (core protein) but now named NV11/2 because it migrates perceptibly faster than V2. Despite a varying background of labeled host proteins, identifiable profiles were obtained for 11 of 12 flaviviruses. The large non-structural proteins NV5 and NV4 migrated at apparently the same rates for all viruses. Profiles of the remaining proteins displayed varying amounts of heterogeneity, notably in the migration of the envelope protein V3 which showed no evidence of subgroup specificity.

摘要

通过在聚丙烯酰胺平板凝胶中进行SDS-磷酸盐电泳，分析了黄病毒在Vero细胞中指定的35S-甲硫氨酸标记蛋白。昆金病毒产生的图谱清晰度使得能够确定非结构蛋白，并确认了NV21/2的身份；该图谱包括一种先前称为V2（核心蛋白）但现在称为NV11/2的蛋白，因为它的迁移速度明显快于V2。尽管标记的宿主蛋白背景各不相同，但12种黄病毒中的11种获得了可识别的图谱。所有病毒的大型非结构蛋白NV5和NV4的迁移速率明显相同。其余蛋白的图谱显示出不同程度的异质性，特别是包膜蛋白V3的迁移，没有显示出亚组特异性的证据。