Protein kinase C alpha, beta immunoreactivity in baker's yeast, lobster and wheat germ.

The immunoreactivity of PKC alpha (protein kinase C alpha) and PKC beta in wheat germ, lobster tail muscle and three strains of yeast was analysed by Western blotting with mouse anti-PKC active fragments. The potency of the immunoreactivity of PKC alpha activity was much greater than that of PKC beta. The occurrence of multiple bands may be due to PKC self-interactions and/or the interactions between PKC and other molecules. The evolutionary conservation of PKC alpha and PKC beta implies that these PKC isoenzymes may play important roles in Ca2+/lipid-dependent signal transduction and cell growth in these eukaryotes.