The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver.

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作者信息

Zetterqvist O, Ragnarsson U, Humble E, Berglund L, Engström L

出版信息

Biochem Biophys Res Commun. 1976 Jun 7;70(3):696-703. doi: 10.1016/0006-291x(76)90648-3.

DOI:10.1016/0006-291x(76)90648-3

PMID:180994

Abstract

摘要

相似文献

The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver.

Biochem Biophys Res Commun. 1976 Jun 7;70(3):696-703. doi: 10.1016/0006-291x(76)90648-3.

Adrenergic control of the cyclic AMP-dependent protein kinase and pyruvate kinase in isolated hepatocytes. Application of a synthetic peptide substrate for measuring protein kinase activity.离体肝细胞中环磷酸腺苷依赖性蛋白激酶和丙酮酸激酶的肾上腺素能控制。用于测量蛋白激酶活性的合成肽底物的应用。

J Biol Chem. 1978 Jul 25;253(14):5147-54.

Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3',5'-AMP-stimulated protein kinase.当用作环3',5'-腺苷酸刺激的蛋白激酶的底物时，对猪肝丙酮酸激酶天然结构的非依赖性。

Biochem Biophys Res Commun. 1975 Sep 16;66(2):614-21. doi: 10.1016/0006-291x(75)90554-9.

Identification of L-type pyruvate kinase as a major phosphorylation site of endogenous cyclic AMP-dependent protein kinase in rat liver soluble fraction.鉴定L型丙酮酸激酶为大鼠肝脏可溶性部分中内源性环磷酸腺苷依赖性蛋白激酶的主要磷酸化位点。

FEBS Lett. 1979 May 15;101(2):289-94. doi: 10.1016/0014-5793(79)81028-5.

Regulation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphorylation reactions, catalyzed by cyclic-AMP dependent protein kinases and a histone phosphatase.

Biochim Biophys Acta. 1976 Jan 23;422(1):98-108. doi: 10.1016/0005-2744(76)90011-5.

Studies on the phosphorylation and dephosphorylation of L-type pyruvate kinase by the catalytic subunit of cyclic AMP-dependent protein kinase.环磷酸腺苷依赖性蛋白激酶催化亚基对L型丙酮酸激酶磷酸化和去磷酸化的研究。

J Biol Chem. 1980 Jan 25;255(2):668-75.

Comparative kinetic studies on the L-type pyruvate kinase from rat liver and the enzyme phosphorylated by cyclic 3', 5'-AMP-stimulated protein kinase.大鼠肝脏L型丙酮酸激酶与经环3',5'-腺苷酸刺激的蛋白激酶磷酸化的该酶的比较动力学研究。

Biochim Biophys Acta. 1976 Apr 8;429(2):374-82. doi: 10.1016/0005-2744(76)90285-0.

Cyclic AMP stimulated phosphorylation of liver pyruvate kinase in hepatocytes.环磷酸腺苷刺激肝细胞中肝丙酮酸激酶的磷酸化。

Biochem Biophys Res Commun. 1978 Dec 14;85(3):900-5. doi: 10.1016/0006-291x(78)90628-9.

Amino acid sequence of a (32P) phosphopeptide from pig liver pyruvate kinase phosphorylated by cyclic 3',5'-AMP-stimulated protein kinase and gamma-(32P)ATP.由环3',5'-AMP刺激的蛋白激酶和γ-(32P)ATP磷酸化的猪肝丙酮酸激酶的(32P)磷酸肽的氨基酸序列

Biochem Biophys Res Commun. 1974 Nov 27;61(2):559-63. doi: 10.1016/0006-291x(74)90993-0.

Phosphorylation of rat kidney pyruvate kinase type L by cyclic 3',5'-AMP-dependent protein kinase.环3',5'-腺苷酸依赖性蛋白激酶对大鼠肾L型丙酮酸激酶的磷酸化作用。

Biochim Biophys Acta. 1978 May 11;524(1):68-77. doi: 10.1016/0005-2744(78)90104-3.

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