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

FEBS Letters

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