Liberation, purification, and properties of thioesterase component of pigeon liver fatty acid synthetase complex
- 1 October 1982
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
- Vol. 713 (1) , 29-38
- https://doi.org/10.1016/0005-2760(82)90163-1
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Use of trypsin and lipoamidase to study the role of lipoic acid moieties in the pyruvate and .alpha.-ketoglutarate dehydrogenase complexes of Escherichia coliBiochemistry, 1981
- Isolation of thioesterase and acyl carrier protein activities liberated by elastase digestion of pigeon liver fatty acid synthetaseBiochemical and Biophysical Research Communications, 1981
- On the Structure of Fatty Acid Synthetase of YeastEuropean Journal of Biochemistry, 1980
- Mammalian fatty acid synthetase: evidence for subunit identity and specific removal of the thioesterase component using elastase digestionFEBS Letters, 1978
- Release of two thioesterase domains from fatty acid synthetase by limited digestion with trypsinBiochemical Journal, 1978
- Evidence for an “active serine” in each fatty acid synthetase peptideBiochemical and Biophysical Research Communications, 1976
- Pantetheine‐Free Mutants of the Yeast Fatty‐Acid‐Synthetase ComplexEuropean Journal of Biochemistry, 1973
- Saturated Fatty Acid Biosynthesis and its RegulationAnnual Review of Biochemistry, 1973
- Acyl Carrier ProteinPublished by Elsevier ,1972
- Fat Metabolism in Higher PlantsPublished by Elsevier ,1964