[Studies on polyamine-dependent protein kinase in pig epidermal cells].
Polyamine-dependent protein kinase (P kinase) in nuclear and cytosol fraction of pig epidermal cells were extracted. Two different protein kinases were purified from nuclei. One was cAMP-dependent protein kinase (A kinase) and another was P kinase. P kinase phosphorylated acidic non-histone protein only, while A kinase phosphorylated both exogenous histone and non-histone proteins. Among polypeptides phosphorylated by P kinase, a 180 kilodalton (K) polypeptide seemed to be a specific substrate for P kinase. In cytosol, the fraction containing P kinase exhibited multiple polypeptide bands on SDS -PAGE, including four major polypeptide bands and several minor polypeptide bands. One of minor polypeptide bands (80 K) was phosphorylated by P kinase. Authentic ornithine decarboxylase (ODC) added exogenously was also phosphorylated by P kinase. A 80 K polypeptide of ODC was comigrated with the polypeptide phosphorylated by P kinase on SDS -PAGE. Kinetic study revealed that the ODC activity decreased as ODC was phosphorylated.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D004592:Electrophoresis, Starch Gel; D000078404:Epidermal Cells; D004817:Epidermis / Q000201:enzymology*; D009955:Ornithine Decarboxylase / Q000032:analysis; D011073:Polyamines / Q000494:pharmacology; D011494:Protein Kinases / Q000032:analysis / Q000378:metabolism*; D013552:Swine
D011073:Polyamines; D011494:Protein Kinases; D009955:Ornithine Decarboxylase