Primary structure of a chymotryptic peptide containing the “active serine” of the thioesterase domain of fatty acid synthase
- 1 November 1981
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 103 (2), 377-382
- https://doi.org/10.1016/0006-291x(81)90463-0
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Chemical modification of an essential lysine at the active site of enoyl-CoA reductase in fatty acid synthetaseArchives of Biochemistry and Biophysics, 1980
- Presence of one essential arginine that specifically binds the 2′-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetaseArchives of Biochemistry and Biophysics, 1980
- The Separation of Dansyl Amino Acids by Reversed-Phase High Performance Liquid ChromatographyJournal of Chromatographic Science, 1978
- Isolation and characterization of a tryptic fragment containing the thioesterase segment of fatty acid synthetase from the uropygial gland of gooseArchives of Biochemistry and Biophysics, 1978
- Thin-Layer Chromatography of Dansyl Amino Acids on PolyamideMicrochimica Acta, 1977
- Control Mechanisms in the Synthesis of Saturated Fatty AcidsAnnual Review of Biochemistry, 1977
- One-step purification and properties of a two-peptide fatty acid synthetase from the uropygial gland of the gooseBiochemistry, 1976
- Evidence for an “active serine” in each fatty acid synthetase peptideBiochemical and Biophysical Research Communications, 1976
- [8] End-group analysis using dansyl chlorideMethods in Enzymology, 1972
- [19] Performic acid oxidationPublished by Elsevier ,1967