Crossref journal-article
Portland Press Ltd.
Biochemical Journal (288)
Abstract

A method was devised to purify branched-chain oxo acid dehydrogenase (BCOAD) from rat kidney which retains endogenous kinase activity. Incorporation of 32P into purified enzyme parallels the time course of enzyme inhibition by ATP. Phosphorylation occurs on a serine residue(s) of the 46000-mol.wt. subunit of the enzyme complex. Endogenous phosphatase activity is not present after purification, and added pyruvate dehydrogenase phosphate phosphatase does not re-activate BCOAD or liberate 32P from previously labelled enzyme. These results demonstrate that BCOAD can be regulated by an endogenous protein kinase and that the phosphorylation-cycle enzymes regulating BCOAD appear to be distinct from those associated with pyruvate dehydrogenase complex.

Bibliography

Odessey, R. (1982). Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity. Biochemical Journal, 204(1), 353–356.

Authors 1
  1. R Odessey (first)
References 0 Referenced 78

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Dates
Type When
Created 10 years ago (Aug. 10, 2015, 4:33 p.m.)
Deposited 3 years, 9 months ago (Nov. 25, 2021, 7:54 a.m.)
Indexed 1 year, 10 months ago (Oct. 31, 2023, 10:49 a.m.)
Issued 43 years, 4 months ago (April 15, 1982)
Published 43 years, 4 months ago (April 15, 1982)
Published Print 43 years, 4 months ago (April 15, 1982)
Funders 0

None

@article{Odessey_1982, title={Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity}, volume={204}, ISSN={0264-6021}, url={http://dx.doi.org/10.1042/bj2040353}, DOI={10.1042/bj2040353}, number={1}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Odessey, R}, year={1982}, month=apr, pages={353–356} }