Isolation of thioesterase and acyl carrier protein activities liberated by elastase digestion of pigeon liver fatty acid synthetase
- 1 June 1981
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 100 (3) , 1010-1016
- https://doi.org/10.1016/0006-291x(81)91924-0
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- 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
- Refinement of the Coomassie blue method of protein quantitationAnalytical Biochemistry, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Acyl Carrier ProteinPublished by Elsevier ,1972
- Comparative Studies of the Pigeon Liver Fatty Acid Synthetase Complex and Its SubunitsJournal of Biological Chemistry, 1970
- Mechanism of dissociation of pigeon liver fatty acid synthetase complex into half-molecular weight subunits and their reassociation to enzymatically active complexBiochemical and Biophysical Research Communications, 1970
- Incorporation of pantothenate-1-14C into pigeon liver fatty acid synthetase: 4′-phosphopantetheine, a prosthetic group of the multienzyme complexArchives of Biochemistry and Biophysics, 1968