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

Publisher Website
Google Scholar
Abstract
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.