Isolation and partial purification of ceruloplasmin messenger RNA from rat liver.
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 X 10(6) 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 X 10(4) daltons as estimated by gel-electrophoresis under denaturating conditions. These values approach the weight of the half-molecule of native ceruloplasmin.
D000818:Animals; D000937:Antigen-Antibody Reactions; D002570:Ceruloplasmin / Q000096:biosynthesis*; D008099:Liver / Q000378:metabolism*; D011061:Poly A / Q000032:analysis; D011132:Polyribosomes / Q000276:immunology / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats
D012333:RNA, Messenger; D011061:Poly A; D002570:Ceruloplasmin