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

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, 45 kDa was...

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Published inFEBS letters Vol. 308; no. 1; pp. 83 - 86
Main Authors Priestman, David A., Mistry, Sharad C., Kerbey, Alan L., Randle, Philip J.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 10.08.1992
Elsevier
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Summary: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, 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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)81056-R