Comparison of the regulatory and catalytic subunits of cAMP dependent protein kinase from Dictyostelium discoideum and bovine heart using polyclonal antibodies.
The purified regulatory (R) and catalytic (C) subunits of cAMP dependent protein kinase (cAK) from the primitive eukaryote Dictyostelium discoideum have been compared with the homologous proteins from bovine heart by SDS-PAGE followed by Western blotting using polyclonal antibodies. No cross-reaction could be demonstrated by this technique although the slime mold subunits share several functional properties with their mammalian counterparts and are able to form functional hybrid holoenzymes.
D000818:Animals; D000941:Antigens / Q000276:immunology*; D002417:Cattle; D003101:Collodion; D000242:Cyclic AMP / Q000494:pharmacology*; D004023:Dictyostelium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007158:Immunologic Techniques; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000276:immunology*; D055503:Protein Multimerization; D013379:Substrate Specificity
D000941:Antigens; D047428:Protein Kinase Inhibitors; D003101:Collodion; D000242:Cyclic AMP; D011494:Protein Kinases