DISTINCT SUBUNITS OF RIBONUCLEOPROTEIN OF INFLUENZA VIRUS
DISTINCT SUBUNITS OF RIBONUCLEOPROTEIN OF INFLUENZA VIRUS
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DOI：
10.1016/0022-2836(69)90237-x
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发表时间：
1969-01-01
影响因子：
5.6
通讯作者：
DUESBERG, PH
中科院分区：
文献类型：
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作者：
DUESBERG, PH
用脱氧胆酸盐、Triton X100或乙醚抽提法将流感病毒A裂解成核糖核蛋白和包膜蛋白。用蔗糖梯度沉降法将核糖核蛋白分为70 s、60 s和50 s组分。聚丙烯酰胺凝胶电泳也得到了病毒核糖核蛋白的三个组分。病毒核蛋白的浮力密度为1.265g/ml。在蔗糖密度梯度中。核糖核蛋白对链霉蛋白酶具有相对抗性。但流感病毒的核糖核蛋白的RNA被RNase降解，在病毒感染细胞后约3小时，可能也检测到相同的三种核糖核蛋白组分。发现流感病毒核蛋白的不同组分含有不同的病毒RNA，这表明它们的异质性是原始的，而不是所用分离程序的人工产物。
Influenza virus A was disrupted by deoxycholate, Triton X100 or ether extraction into ribonucleoprotein and envelope proteins. The ribonucleoprotein was resolved into a 70 s, a 60 s and a 50 s component by sucrose gradient sedimentation. Three components of viral ribonucleoprotein were also obtained by polyacrylamide gel electrophoresis. The buoyant density of the viral nucleoprotein was 1.265 g/ml. in a sucrose density-gradient. The ribonucleoprotein was relatively resistant to pronase. But the RNA of the ribonucleoproteins of influenza virus was degraded by RNase.Probably the same three ribonucleoprotein components were also detected in virus-infected cells about three hours after infection. Distinct components of the influenza virus nucleoprotein were found to contain distinct viral RNA's, suggesting that their heterogeneity is original and not an artifact of the isolation procedures used.