Literature DB >> 3619032

Purification of branched chain alpha-ketoacid dehydrogenase complex from rat liver.

Y Shimomura, R Paxton, T Ozawa, R A Harris.   

Abstract

A new method using hydrophobic interaction chromatography on phenyl-Sepharose was developed to purify branched chain alpha-ketoacid dehydrogenase complex from commercially available frozen rat liver. Yields of greater than 50% were routinely achieved. The purified enzyme, composed of E1 alpha, E1 beta, 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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Year:  1987        PMID: 3619032     DOI: 10.1016/0003-2697(87)90094-7

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  3 in total

1.  Production of recombinant E1 component of branched-chain alpha-keto acid dehydrogenase complex.

Authors:  J W Hawes; Y Zhao; K M Popov; Y Shimomura; R A Harris
Journal:  Methods Enzymol       Date:  2000       Impact factor: 1.600

2.  Preservation of the activity state of hepatic branched-chain 2-oxo acid dehydrogenase during the isolation of mitochondria.

Authors:  B Zhang; R Paxton; G W Goodwin; Y Shimomura; R A Harris
Journal:  Biochem J       Date:  1987-09-15       Impact factor: 3.857

3.  Gene expression profiling of mice with genetically modified muscle glycogen content.

Authors:  Gretchen E Parker; Bartholomew A Pederson; Mariko Obayashi; Jill M Schroeder; Robert A Harris; Peter J Roach
Journal:  Biochem J       Date:  2006-04-01       Impact factor: 3.857

  3 in total

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