Phosphorylation sites and inactivation of branched-chain α-ketoacid dehydrogenase isolated from rat heart, bovine kidney, and rabbit liver, kidney, heart, brain, and skeletal muscle
- 1 January 1986
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 244 (1) , 187-201
- https://doi.org/10.1016/0003-9861(86)90108-6
Abstract
No abstract availableThis publication has 24 references indexed in Scilit:
- Regulation of bovine kidney branched-chain 2-oxoacid dehydrogenase complex by reversible phosphorylationEuropean Journal of Biochemistry, 1984
- Multi‐site phosphorylation in ox‐kidney branched‐chain 2‐oxoacid dehydrogenase complexFEBS Letters, 1983
- Activity state of the branched chain α-ketoacid dehydrogenase complex in heart, liver, and kidney of normal, fasted, diabetic, and protein-starved ratsBiochemical and Biophysical Research Communications, 1983
- Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activityBiochemical Journal, 1982
- Incorporation of [32P]phosphate into the pyruvate dehydrogenase complex in rat heart mitochondriaBiochemical Journal, 1980
- Amino acid sequences around the sites of phosphorylation in the pig heart pyruvate dehydrogenase complexBiochemical Journal, 1979
- Regulation of kinase reactions in pig heart pyruvate dehydrogenase complexBiochemical Journal, 1979
- Function of phosphorylation sites on pyruvate dehydrogenaseBiochemical and Biophysical Research Communications, 1979
- Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heartBiochemistry, 1978
- Peptides derived from pyruvate dehydrogenase as substrates for pyruvate dehydrogenase kinase and phosphataseBiochemical and Biophysical Research Communications, 1977