PHOSPHORYLATION OF MITOCHONDRIAL PROTEINS IN BOVINE HEART - CHARACTERIZATION OF KINASES AND SUBSTRATES

被引：39

作者：

TECHNIKOVADOBROVA, Z ^{[1
]}

SARDANELLI, AM ^{[1
]}

PAPA, S ^{[1
]}

机构：

[1] CZECHOSLOVAK ACAD SCI, INST MICROBIOL, CS-11142 PRAGUE 1, CZECHOSLOVAKIA

来源：

FEBS LETTERS | 1993年 / 322卷 / 01期

关键词：

MITOCHONDRION; PROTEIN PHOSPHORYLATION; PROTEIN KINASE; CYCLIC AMP; CYCLIC AMP-DEPENDENT PROTEIN KINASE;

D O I：

10.1016/0014-5793(93)81109-D

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：

Protein phosphorylation by [gamma-P-32]ATP in total extract and subfractions of bovine heart mitochondria has been studied. The results show that, in addition to pyruvate dehydrogenase, three mitochondrial proteins, with molecular weights of 44,000, 39,000 and 31,000 Da, are phosphorylated by a cAMP-independent mitochondrial protein kinase. Three other proteins associated with mitochondria, with molecular weights of 125,000, 19,000 and 6,500 Da, are phosphorylated by the cytoplasmic cAMP-dependent protein kinase (kinase A).

引用

页码：51 / 55

页数：5

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