The effect of the cAMP-dependent protein kinase on protein phosphorylation and phosphatidylinositol 4-phosphate formation in a hepatocyte membrane preparation.
Plasma membrane preparation obtained from isolated mouse hepatocytes was phosphorylated by exogenous cyclic AMP dependent protein kinase in the presence of 32P-ATP. The phosphorylated proteins were analysed by SDS-polyacrylamide gel-electrophoresis of the membrane and the phosphorylated lipids were analysed by thin layer chromatography of the separated lipid fraction. The protein kinase stimulated the 32P incorporation into phosphatidylinositol 4-phosphate and it catalyzed the phosphorylation of several proteins. The main phosphoprotein bands were found at 51 kDa, 49 kDa, 46 kDa and 34 kDa. A part of the 51 kDa phosphoprotein accompanied the lipids in the course of the separation of the lipid fraction.
Mészáros
G
G
1st Institute of Biochemistry, Semmelweis University Medical School, Budapest, Hungary.
Enyedi
A
A
Bánhegyi
G
G
Mandl
J
J
Antoni
F
F
Faragó
A
A
D000818:Animals; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D051379:Mice; D008815:Mice, Inbred Strains; D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*
D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols; D011506:Proteins; C037178:phosphatidylinositol 4-phosphate; D011494:Protein Kinases