Isolation and partial purification of ceruloplasmin messenger RNA from rat liver |
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Authors: | S. A. Neifakh V. S. Gaitskhoki N. A. Klimov L. V. Puchkova M. M. Shavlovski A. L. Schwartzman |
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Affiliation: | (1) Laboratory of Biochemical Genetics of the Institute of Experimental Medicine, Leningrad, U.S.S.R. |
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Abstract: | Partially purified ceruloplasmin mRNA was isolated using indirect immunoprecipitation of rat liver polysomes and poly(U)-Sepharose chromatography of polysomal RNA. This RNA programmed the synthesis of ceruloplasmin polypeptides in a cell-free system from mitochondria. Immunochemical analysis of the translation products revealed a 40-fold enrichment of the ceruloplasmin mRNA activity. The purified ceruloplasmin mRNA migrated as a major homogeneous component with an apparent molecular weight about 1×106 daltons in polyacrylamide gels containing sodium dodecyl sulfate. The immunoprecipitated products of the cell-free translation had molecular weights in the range 4.5–5.4×104 daltons as estimated by gel-electrophoresis under denaturating conditions. These values approach the weight of the half-molecule of native ceruloplasmin. |
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