FURTHER EVIDENCE FOR MULTIPLE PROTEINS IN FOOT-AND-MOUTH DISEASE VIRUS PARTICLE
FURTHER EVIDENCE FOR MULTIPLE PROTEINS IN FOOT-AND-MOUTH DISEASE VIRUS PARTICLE
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DOI：
10.1099/0022-1317-13-1-73
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发表时间：
1971-01-01
影响因子：
3.8
通讯作者：
BROWN, F
中科院分区：
文献类型：
--
作者：
BURROUGHS, JN;ROWLANDS, DJ;BROWN, F
已获得进一步证据，证实口蹄疫病毒含有几种结构蛋白。通过尿素-聚丙烯酰胺凝胶电泳，O型病毒有6条不同的条带。在十二烷基硫酸钠-聚丙烯酰胺凝胶中，可以清楚地发现分子量分别为34、30、26和13.5 × 103的四种蛋白质。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和尿素-聚丙烯酰胺凝胶电泳中，用单个氨基酸标记病毒制剂时，迁移最快的蛋白质不含精氨酸，只有微量半胱氨酸。该蛋白在考马斯蓝染色下也与其他条带不同，并且在温和酸（pH 6.5）破坏病毒制备的12s蛋白亚基中不存在。在AmberIite IRC-50上通过蔗糖梯度离心和离子交换层析从12s亚基中分离出该蛋白。
Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylamide gels four proteins with molecular weights of 34, 30, 26 and 13.5 × 103were clearIy demonstrated. When virus preparations were labelled with a single amino acid, in both sodium dodecyl sulphate-polyacrylamide and urea-polyacrylamide gel electrophoresis, the fastest migrating protein contained no arginine and only traces of cysteine. This protein also stained differently from the other bands with Coomassie Blue and was absent from the 12s protein subunit prepared by mild acid (pH 6.5) disruption of the virus. This protein was separated from the 12s subunit by sucrose gradient centrifugation and by ion exchange chromatography on AmberIite IRC-50.