PURIFICATION AND PARTIAL CHARACTERIZATION OF RAT-LIVER PYRUVATE-DEHYDROGENASE KINASE ACTIVATOR PROTEIN (FREE PYRUVATE-DEHYDROGENASE KINASE)

被引：24

作者：

PRIESTMAN, DA ^{[1
]}

MISTRY, SC ^{[1
]}

KERBEY, AL ^{[1
]}

RANDLE, PJ ^{[1
]}

机构：

[1] UNIV OXFORD,JOHN RADCLIFFE HOSP,DEPT CLIN BIOCHEM,OXFORD OX3 9DU,ENGLAND

来源：

FEBS LETTERS | 1992年 / 308卷 / 01期

关键词：

PYRUVATE DEHYDROGENASE KINASE; RAT LIVER MITOCHONDRIA; STARVATION; N-TERMINAL SEQUENCE; SPECIFIC ACTIVITY;

D O I：

10.1016/0014-5793(92)81056-R

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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(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.

引用

页码：83 / 86

页数：4

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