Premium
Phosphorylation of type‐L pyruvate kinase in intact hepatocytes Localisation of the phosphorylation site in response to both glucagon and the Ca 2+ ‐linked agonist phenylephrine
Author(s) -
Hsu Ying Chang,
Bloxham David P.,
Giles Ian G.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81006-2
Subject(s) - phosphorylation , glucagon , pyruvate kinase , chemistry , biochemistry , protein kinase a , agonist , biology , enzyme , endocrinology , medicine , hormone , receptor , glycolysis
Pyruvate kinase is one of the enzymes which can be phosphorylated by stimulation of the cell with either glucagon or Ca 2+ ‐linked hormones. Whether these two classes of hormones phosphorylate the same site on the enzyme is unclear. Our results demonstrate that isolation of [ 32 P]phosphorylated type‐L pyruvate kinase from glucagon‐treated hepatocytes followed by aspartyl‐prolyl cleavage yields a [ 32 P]phosphorylated peptide of M r 17000. This fragment is also phosphorylated in response to the Ca 2+ ‐mediated agonist phenylephrine.