期刊论文详细信息
FEBS Letters | |
Phosphorylation of type‐L pyruvate kinase in intact hepatocytes Localisation of the phosphorylation site in response to both glucagon and the Ca2+‐linked agonist phenylephrine | |
Giles, Ian G.1  Bloxham, David P.2  Hsu, Ying Chang1  | |
[1] Department of Biochemistry, School of Biochemical and Physiological Sciences, University of Southampton, Bassett Crescent East, Southampton SO9 3TU, England;Roche Products Ltd, PO Box 8, Welwyn Garden City AL7 3AY, England | |
关键词: Pyruvate kinase; Phosphorylation; Glucagon; Phenylephrine; Phosphorylation site; Aspartyl-prolyl deavage; | |
DOI : 10.1016/0014-5793(87)81006-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Pyruvate kinase is one of the enzymes which can be phosphorylated by stimulation of the cell with either glucagon or Ca2+-linked hormones. Whether these two classes of hormones phosphorylate the same site on the enzyme is unclear. Our results demonstrate that isolation of [32P]phosphorylated type-L pyruvate kinase from glucagon-treated hepatocytes followed by aspartyl-prolyl cleavage yields a [32P]phosphorylated peptide of M r 17000. This fragment is also phosphorylated in response to the Ca2+-mediated agonist phenylephrine.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020289359ZK.pdf | 623KB | download |