Goose fatty acid synthetase mRNA.

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Goose fatty acid synthetase mRNA.

The fatty acid synthetase of animal tissues consists of two identical subunits (Mr = 250,000), each of which is a multienzyme protein containing domains for the acyl carrier peptide and the seven different catalytic activities required for the conversion of acetyl-CoA and malonyl-CoA to palmitate. Total poly(A+) RNA was isolated from goose uropygial gland and translated in a cell-free rabbit re...

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Regulation of synthesis of hepatic fatty acid synthetase: binding of fatty acid synthetase antibodies to polysomes.

Mammalian fatty acid synthetase was shown to be composed of two peptides, molecular weight 240,000, after dissociation with sodium dodecyl sulfate. Rat liver polysomes that synthesize fatty acid synthetase were identified by sucrose gradient analysis of polysomes that had been reacted with 125I-labeled antibody against fatty acid synthetase. The binding of 125I-labeled antibody to polysomes was...

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Fatty acid synthetase from Chlamydomonas reinhardi.

Cell-free extracts of the unicellular green alga, Chlnmydomonas reinhardi, catalyze the incorporation of acetyl-CoA and malonyl-CoA into long chain fatty acids. The fatty acid synthetase is dependent on added acyl carrier protein for activity, regardless if the cells are grown in the light or in the dark. The major products formed from acetyl-CoA and malonyl-CoA by cells in the light period of ...

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Fatty acid synthetase of Saccharomyces cerevisiae.

A light particle fraction of Saccharomyces cerevisiae, obtained from the crude ribosomal material, and containing the fatty acid synthetase, consisted primarily of 27S and 47S components. This fraction has a protein-ribonucleic acid ratio of about 13. Electron micrographs showed particles ranging in diameter between 100 and 300 A in this material. By use of density gradient analysis, the fatty ...

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Regulation of Fatty Acid Synthetase Activity

The 4’-phosphopantetheine hyd.rolase of rat liver, partially purified by ammonium sulfate precipitation, catalyzes the hydrolysis of the prosthetic group 4’phosphopantetheine from the holo-fatty acid synthetase. The two products of the action of this enzyme, 4’phosphopantetheine and apo-fatty acid synthetase, were isolated by DEAE-cellulose chromatography and by chromatography on a Sepharose e-...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1980

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)43418-7