Preparations of tobacco etch virus (TEV) RNA which were purified by sucrose gradient centrifugation, digested with RNase, and analyzed by SDS-polyacrylamide gel electrophoresis contained proteins of 49, 32, and 24 kDa. The 49and 24-kDa proteins reacted with polyclonal antiserum to the TEV 49-kDa proteinase while the 32-kDa protein reacted with anti-TEV serum. Further purification of the RNA by centrifugation through CsCl removed the coat protein (32 kDa), but not the 49- and 24-kDa proteins. The 49- and 24-kDa proteins did not migrate into a polyacrylamide gel when the RNA was not digested with RNase. These results indicate that the VPg of TEV is either the 49-kDa proteinase or the 24 kDa that represents the amino-terminal half thereof.
|Number of pages||4|
|State||Published - Sep 1990|
Bibliographical noteFunding Information:
We thank Wrlliam G. Dougherty for providing polyclonal and monoclonal antisera to the 49.kDa proternase and Thomas P. Pirone for provrding antrserum to TEV. This work was supported by Grant 4E021 from the Unrversrty of Kentucky Tobacco and Health Research Institute and Grant 85.CRCR-1-1536 from the U.S. Department of Agriculture Competitive Grants Program.
Copyright 2014 Elsevier B.V., All rights reserved.
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