The flux through branched-chain a-ketoacid dehydrogenase and the activity of the branched-chain a-ketoacid dehydrogenase complex were measured in hepatocytes isolated from fed, starved and alloxan diabetic rats. The highest rate of branched-chain a-ketoacid oxidation was found in hepatocytes isolate
Purification of branched chain α-ketoacid dehydrogenase complex from rat liver
✍ Scribed by Yoshiharu Shimomura; Ralph Paxton; Takayuki Ozawa; Robert A. Harris
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 452 KB
- Volume
- 163
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A new method using hydrophobic interaction chromatography on phenyl-Sepharose was developed to purify branched chain Lu-ketoacid dehydrogenase complex from commercially available frozen rat liver. Yields of greater than 50% were routinely achieved. The purified enzyme, composed of Elc~, El& and E2 subunits, appeared homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and contained endogenous kinase activity for phosphorylation and inactivation of the complex.
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