期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1978
卷号：75
期号：6
页码：2722-2726
DOI：10.1073/pnas.75.6.2722
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
