Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase

D. G. Morgan, A. Routtenberg

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

Phosphorylation of a brain protein of Mr=41,000, termed band F2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F2 on polyacrylamide gels and both appear as a doublet band of Mr=41,000−42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function.

Original languageEnglish (US)
Pages (from-to)569-576
Number of pages8
JournalTopics in Catalysis
Volume95
Issue number2
DOIs
StatePublished - Jan 1 1980

Keywords

  • apparent molecular weight
  • M
  • SDS
  • Sodium dodecyl sulfate

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Biophysics
  • Molecular Biology

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