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- W1858035622 abstract "Research Article1 April 1982free access Purification of mRNA guanylyltransferase from calf thymus. Y. Nishikawa Y. Nishikawa Search for more papers by this author P. Chambon P. Chambon Search for more papers by this author Y. Nishikawa Y. Nishikawa Search for more papers by this author P. Chambon P. Chambon Search for more papers by this author Author Information Y. Nishikawa and P. Chambon The EMBO Journal (1982)1:485-492https://doi.org/10.1002/j.1460-2075.1982.tb01195.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info mRNA guanylyltransferase has been extensively purified from calf thymus. A GTP-binding assay was used based on the observations by Shuman and Hurwitz (1981) and Venkatesan and Moss (1982) that vaccinia virus and HeLa cell mRNA guanylyltransferases bind the GMP moiety from GTP in the absence of an acceptor RNA. The mol. wt. of the purified enzyme from calf thymus, estimated by polyacrylamide gel electrophoresis in the presence of SDS, is 65 000. The major protein in the purified enzyme fraction comigrates with the peptide labelled with GMP. Based on scans of silver-stained polyacrylamide gels, mRNA guanylyltransferase constitutes greater than 50% of the protein in these fractions. The enzyme catalyzed the guanylylation at the 5′ end of poly(A) with a mixture of diphosphate and triphosphate ends. No evidence was obtained for a direct interaction between mRNA guanylyltransferase and RNA polymerase B (II). Previous ArticleNext Article Volume 1Issue 41 April 1982In this issue RelatedDetailsLoading ..." @default.
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- W1858035622 title "Purification of mRNA guanylyltransferase from calf thymus." @default.
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