Solubilization and partial purification of an enzyme involved in rat liver microsomal fatty acid chain elongation: beta-hydroxyacyl-CoA dehydrase.
Open Access
- 1 November 1979
- journal article
- abstracts
- Published by Elsevier
- Vol. 254 (22) , 11584-11590
- https://doi.org/10.1016/s0021-9258(19)86525-0
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Mechanism of rat liver microsomal stearyl-CoA desaturase. Studies of the substrate specificity, enzyme-substrate interactions, and the function of lipid.Published by Elsevier ,2021
- The enzymic chain elongation of fatty acids by rat-liver microsomesPublished by Elsevier ,2002
- Control Mechanisms in the Synthesis of Saturated Fatty AcidsAnnual Review of Biochemistry, 1977
- Chemistry and Biochemistry of Unsaturated Fatty AcidsAngewandte Chemie International Edition in English, 1976
- Purification and Properties of Rat Liver Microsomal Stearyl Coenzyme A DesaturaseProceedings of the National Academy of Sciences, 1974
- On the Mechanism and Control of the Malonyl‐CoA‐Dependent Chain Elongation of Fatty AcidsEuropean Journal of Biochemistry, 1974
- Membrane-bound enzymes and membrane ultrastructureBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1973
- Mechanisms and physiological roles of fatty acid chain elongation in microsomes and mitochondriaMolecular and Cellular Biochemistry, 1973
- The Fluid Mosaic Model of the Structure of Cell MembranesScience, 1972
- ENZYMES OF THE FATTY ACID CYCLE. II. ETHYLENE REDUCTASE1Journal of the American Chemical Society, 1953