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

FEBS Letters

Randle, Philip J.¹  Mistry, Sharad C.¹  Kerbey, Alan L.¹  Priestman, David A.¹ 

[1] Department of Clinical Biochemistry, University of Oxford, John Radeliffe Hospital, Oxford, OX3 9DU, UK

关键词: Pyruvate dehydrogenase kinase;    Rat liver mitochondria;    Starvation;    N-terminal sequence;    Specific activity;    PDH;    pyruvate dehydrogenase;    KAP;    kinase activator protein;    cAMP;    adenosine 3′;    5′ phosphate;    PDH-E1;    PDH-E2;    E1 and E2 components of PDH complex;   

DOI  :  10.1016/0014-5793(92)81056-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown