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Polyclonal antibodies raised against a highly conserved region of the catalytic subunit of the rat type-C protein kinase cross-reacted with the human type-C protein kinase, but not with the human type-A or type-B protein kinases. By immunoblotting experiments on rat liver extracts, the protein kinase was detected in the nuclei with a discrete pattern depending on the age of the rat. In younger rats (2 weeks old), the antibody recognized a prominent doublet corresponding to 75 and 76 kDa polypeptides and a weaker band of 52 kDa, while in the liver of older rats (12 months old), the antibodies revealed three protein bands, 90, 65 and 60 kDa. On immunofluorescence experiments, the protein kinase was localized in the nuclei of hepatocytes, hepatoma Fao, HTC hepatoma and non-activated Kupffer cells. The catalytic subunit of the type-C protein kinase was immunocytochemically localized in nuclei of rat hepatocytes and in nucleoli of hepatoma Fao cells. The complex formation of the protein kinase and its catalytic subunit to the nucleoli was demonstrated by a co-immunofluorescence technique. The phosphorylation pattern of three proteins, including the p52 protein, in the nuclei of the rat liver was investigated by autoradiography after incubation of the liver slices with [gamma-32P]ATP. There was a good correlation between this autoradiographic pattern and