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Regulation of synthesis of hepatic fatty acid synthetase: polysomal translation in a cell-free system.
Author(s) -
Arnold W. Strauss,
Alfred W. Alberts,
Sally W. Hennessy,
P. Roy Vagelos
Publication year - 1975
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.11.4366
Subject(s) - polysome , immunoprecipitation , biochemistry , fatty acid , biology , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , gel electrophoresis , cell free system , fatty acid synthesis , translation (biology) , protein biosynthesis , protein subunit , enzyme , ribosome , messenger rna , rna , gene
Polysomes were isolated from livers of rats fed various diets and were translated in a protein-synthesizing system derived from cultured Chang liver cells. One of the labeled products was identified as complete subunit(s) of fatty acid synthetase by indirect immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the solubilized immunoprecipitate. The relative amounts of fatty acid synthetase synthesized by polysomes from livers of rats fed a normal diet, starved rats, and rats starved and refed a fat-free diet for 16 hr were 1, 0.1, and 10, respectively. Induction of synthesis of fatty acid synthetase after fat-free refeeding of starved rats began by 2 hr (3-fold increase over starved animals), was increasing rapidly by 5 hr (19-fold over starved animals), and reached a high level by 16 hr (95-fold over starved and 10-fold over normally fed).

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