Isolation of thioesterase and acyl carrier protein activities liberated by elastase digestion of pigeon liver fatty acid synthetase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Mechanism of dissociation of pigeon liver fatty acid synthetase complex into half-molecular weight subunits and their reassociation to enzymatically active complex
2. Comparative Studies of the Pigeon Liver Fatty Acid Synthetase Complex and Its Subunits
3. Mammalian fatty acid synthetase: evidence for subunit identity and specific removal of the thioesterase component using elastase digestion
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1. The Multifunctional Polypeptide Chains of Rabbit-Mammary Fatty-Acid Synthase;European Journal of Biochemistry;2005-03-03
2. Pantothenic Acid in Health and Disease;Vitamins & Hormones;1991
3. Isolation, purification, and characterization of a peptide that contains the β-ketoacyl reductase, enoyl reductase, and β-hydroxyacyl dehydrase activities of the pigeon liver fatty acid synthetase;Canadian Journal of Biochemistry and Cell Biology;1985-01-01
4. Fatty acid synthase — an example of protein evolution by gene fusion;Trends in Biochemical Sciences;1984-02
5. Chapter 2 Animal and bacterial fatty acid synthetase: structure, function and regulation;Fattv Acid Metabolism and Its Regulation;1984
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