Purification and partial characterization of rat liver pyruvate dehydrogenase kinase activator protein (free pyruvate dehydrogenase kinase)

D A Priestman; S C Mistry; A L Kerbey; P J Randle

doi:10.1016/0014-5793(92)81056-r

Purification and partial characterization of rat liver pyruvate dehydrogenase kinase activator protein (free pyruvate dehydrogenase kinase)

FEBS Lett. 1992 Aug 10;308(1):83-6. doi: 10.1016/0014-5793(92)81056-r.

Authors

D A Priestman¹, S C Mistry, A L Kerbey, P J Randle

Affiliation

¹ Department of Clinical Biochemistry, University of Oxford, John Radcliffe Hospital, UK.

PMID: 1644204
DOI: 10.1016/0014-5793(92)81056-r

Abstract

Rat liver pyruvate dehydrogenase (PDH) kinase activator protein (KAP), a free PDH kinase readily separable from PDH complex and its intrinsic kinase, has been purified to apparent homogeneity from liver mitochondria of fed and 48-h starved rats. On SDS-PAGE an apparently single band of M(r) 45 kDa was obtained. N-Terminal amino acid sequence analyses (8-10 cycles) confirmed the presence of a single peptide in each case. The specific activity of the purified KAP from 48-h starved rats (14,413 U/mg protein) was 4.5-fold greater than that from fed rats.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Chromatography, Liquid
Electrophoresis, Polyacrylamide Gel
Mitochondria, Liver / enzymology*
Molecular Sequence Data
Protein Kinases / isolation & purification*
Protein Kinases / metabolism
Protein Serine-Threonine Kinases
Pyruvate Dehydrogenase Acetyl-Transferring Kinase
Rats
Starvation / enzymology

Substances

Pyruvate Dehydrogenase Acetyl-Transferring Kinase
Protein Kinases
Protein Serine-Threonine Kinases