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Purification and partial characterization of rat liver pyruvate dehydrogenase kinase activator protein (free pyruvate dehydrogenase kinase)
Author(s) -
Priestman David A.,
Mistry Sharad C.,
Kerbey Alan L.,
Randle Philip J.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81056-r
Subject(s) - pyruvate dehydrogenase kinase , pyruvate dehydrogenase phosphatase , pyruvate dehydrogenase complex , pyruvate kinase , pkm2 , biochemistry , pyruvate dehydrogenase lipoamide kinase isozyme 1 , activator (genetics) , pyruvate decarboxylation , microbiology and biotechnology , enzyme , protein kinase a , lactate dehydrogenase , chemistry , biology , glycolysis , receptor
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.