[A comparative analysis of chromatographic, kinetic and antigenic properties of casein kinase type 2 from bovine liver and the phytopathogenic mushroom Verticillium dahliae].

Homogeneous preparations of casein kinases 2 have been isolated from bovine liver and the phytopathogenic fungus Verticillium dahliae. The isolation procedure was similar in both cases and included consecutive chromatography on heparin-Sepharose, phosphocellulose PII and monoQ. The bovine liver enzyme consists of two subunits with molecular masses of 38 kDa and 27 kDa, while the fungus kinase has three subunits with Mr of 53 kDa, 41 kDa and 38 kDa. Self-phosphorylation of casein kinase 2 in vitro resulted in phosphate incorporation into the smaller subunit of the mammalian enzyme and into all the three subunits of the fungal enzyme. The Km value of casein kinase 2 from bovine liver for ATP is 3.1 microM; that for GTP is 22.0 microM. The corresponding parameters of the fungal kinase are 14.3 and 18.2 microM, respectively. Specific antibodies to each kinase have been raised. The lack of antigenic cross-reactions between the two enzymes has been demonstrated by ELISA.