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pubmed-article:2847734pubmed:abstractTextRabbit muscle polyA+ mRNA was translated in vitro using a rabbit reticulocyte lysate system in the presence of [35S]methionine. A mouse monoclonal antibody to the catalytic subunit of rabbit muscle phosphorylase phosphatase ("phosphatase C-I") was used to immunoprecipitate the products which were then analyzed by SDS-PAGE and autoradiography. These studies showed that the major product of the phosphatase mRNA is a single ca. 36 kDa polypeptide. These findings are significant in view of suggestions that the catalytic subunit is derived from a larger precursor, and in view of the molecular cloning of two cDNAs for the phosphatase, which encode polypeptides of 35.4 kDa and 37.5 kDa, respectively.lld:pubmed
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pubmed-article:2847734pubmed:authorpubmed-author:LeeE YEYlld:pubmed
pubmed-article:2847734pubmed:authorpubmed-author:ZhengS YSYlld:pubmed
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pubmed-article:2847734pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:2847734pubmed:articleTitleImmunoprecipitation of the in vitro translation product of rabbit muscle protein phosphatase C-I mRNA.lld:pubmed
pubmed-article:2847734pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101.lld:pubmed
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