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A tandem chromatographic column method for assaying cAMP-dependent protein kinase and protein kinase C with synthetic peptide substrates.

作者信息

Egan J J, Chang M K, Londos C

机构信息

Membrane Regulation Section, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892.

出版信息

Anal Biochem. 1988 Dec;175(2):552-61. doi: 10.1016/0003-2697(88)90583-0.

DOI:10.1016/0003-2697(88)90583-0
PMID:3071188
Abstract

A method was devised for assaying protein kinases that phosphorylate either Kemptide, such as cAMP-dependent protein kinase, or a glycogen synthase peptide, which is an excellent substrate for protein kinase C. Upon sequential processing of reaction mixtures through tandem columns of cation and anion exchange resins, radioactivity in background samples is nearly nil and the yield of phosphorylated peptides is high. This method reduces labor, radioactivity, enzyme requirements, and costs of assaying protein kinases.

摘要

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Proc Natl Acad Sci U S A. 1990 Feb;87(3):1052-6. doi: 10.1073/pnas.87.3.1052.
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Phosphorylation state of the GLUT4 isoform of the glucose transporter in subfractions of the rat adipose cell: effects of insulin, adenosine, and isoproterenol.大鼠脂肪细胞亚组分中葡萄糖转运蛋白GLUT4亚型的磷酸化状态：胰岛素、腺苷和异丙肾上腺素的作用。
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