Protein synthesis with membrane-bound polysomes and albumin messenger RNA from livers of mutant mice.

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Investigation of deficiencies in serum protein synthesis resulting from deletion-mutations at the albino locus in mice was continued using in vitro conditions. Previous work showed that although total protein synthesis was only slightly lower in livers from albinos, newly synthesized protein appearing in plasma was 22% of that in controls. It was thought that the disorganized endoplasmic reticulum and Golgi apparatus, characteristic for the liver (and kidney) of these mutants, might be responsible for the observed deficiencies. In the present study membrane-bound polysomes isolated from the livers of newborn albinos were 55% (c3H/c3H strain) and 62% (c14CoS strain) as efficient as those from normal littermates in incorporating radioactive leucine into protein in a cell-free system. These differences could not be eliminated by the addition of excess liver mRNA, exogenous soluble factors or by the exchange of cell sap between albino and control polysomes. In an earlier study albino liver slices synthesized only 13% (or 17% per mg of total protein synthesized) as much albumin as controls. We have now found that the level of albumin poly(A)+-RNA isolated from albino livers assayed with a reticulocyte lysate, was almost as high (85%) as in controls. It was concluded that the very low level of albumin in albino livers did not result from a deficiency of albumin mRNA. Whether the rate-limiting step in synthesis of albumin in mutant livers is at the level of translation or processing for secretion requires further investigation.