辛德毕斯病毒结构蛋白的氨基末端序列分析
Amino-terminal sequence analysis of the structural proteins of Sindbis virus.
作者信息
Bell J R, Hunkapiller M W, Hood L E, Strauss J H
出版信息
Proc Natl Acad Sci U S A. 1978 Jun;75(6):2722-6. doi: 10.1073/pnas.75.6.2722.
Abstract
The structural proteins of Sindbis virus, an enveloped virus which belongs to the Togavirus family, have been subjected to automated Edman degradation using improved techniques. Extensive NH2-terminal sequences of about 50 residues were determined for each of the two membrane glycoproteins. In both cases the NH2 terminus of the molecule was found to be similar in composition to typical water-soluble proteins. The viral capsid protein was found to have a blocked alpha-amino group. This is consistent with other observations that viral proteins derived from the NH2 terminus of precursor molecules are often blocked.
摘要
辛德毕斯病毒是一种包膜病毒，属于披膜病毒科，其结构蛋白已使用改进技术进行了自动埃德曼降解。已确定了两种膜糖蛋白中每种蛋白约50个残基的广泛氨基末端序列。在这两种情况下，均发现分子的氨基末端在组成上与典型的水溶性蛋白质相似。发现病毒衣壳蛋白具有封闭的α-氨基。这与其他观察结果一致，即源自前体分子氨基末端的病毒蛋白通常是封闭的。
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