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- W1981128375 abstract "Abstract Free and membrane-bound polyribosomes and their respective mRNAS were isolated from the livers of both normal rats and rats treated with a single large dose of iron a few hours before being killed. The membrane-bound and free polysomes were incubated in vitro with [ 3 H]leucine and a pH 5 enzyme preparation, and peptide chains of albumin and ferritin were identified by immunoprecipitation. Albumin peptide chains were almost completely confined to the bound ribosomes, whereas ferritin peptide chains were found three times more frequently on free ribosomes than on bound ribosomes. Messenger RNA from each class of ribosome was translated in a wheat germ system, and the products were isolated by immunoprecipitation. Albumin mRNA was restricted almost exclusively to membrane-bound ribosomes. However, ferritin mRNA was equally abundant in the total mRNA of bound and free ribosomes. This finding contrasts with the low capacity of the bound ribosomes to synthesize ferritin in vitro, and suggests that the bound ribosomes of liver contain non-translated ferritin mRNA. Brief treatment of the rats with iron caused a sharp increase in the amount of nascent ferritin chains and l -ferritin mRNA in the free liver ribosomes, but failed to change the nascent chains or ferritin mRNA content of the bound polyribosome fraction. Only an apoferritin subunit of 19 000 daltons was formed by the free and membrane-bound ferritin mRNA. This has significance for the published observation of several sizes of protein subunits in ferritin isolated from tissue ferritins. These may represent modifications of the peptide chain after translation or artifacts of isolation." @default.
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- W1981128375 date "1977-01-01" @default.
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- W1981128375 title "Distribution of ferritin mRNA and albumin mRNA between free and membrane-bound rat liver polysomes" @default.
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- W1981128375 doi "https://doi.org/10.1016/0005-2787(77)90198-8" @default.
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