Nuclear protein kinase activity in glucagon-stimulated perfused rat livers.
Nuclei isolated from glucagon-stimulated perfused rat livers contained 2-3 times as much protein kinase activity as did nuclei from control animals. In the presence of either the heat-stable inhibitor or the protein kinase regulatory subunit the elevated cyclic AMP-independent enzyme activity from stimulated nuclei was inhibited to an activity equivalent to that found in controls.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D000242:Cyclic AMP; D003593:Cytoplasm; D005934:Glucagon / Q000494:pharmacology*; D006358:Hot Temperature; D066298:In Vitro Techniques; D007770:L-Lactate Dehydrogenase; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D010477:Perfusion; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D005934:Glucagon; D000242:Cyclic AMP; D007770:L-Lactate Dehydrogenase; D011494:Protein Kinases