The immunoreactivity of PKCalpha(protein kinase C-alpha) and PKCbeta i
n wheat germ, lobster tail muscle and three strains of yeast was analy
sed by Western blotting with mouse anti-PKC active fragments. The pote
ncy of the immunoreactivity of PKCalpha activity was much greater than
that of PKCbeta. The occurrence of multiple bands may be due to PKC s
elf-interactions and/or the interactions between PKC and other molecul
es. The evolutionary conservation of PKCalpha and PKCbeta implies that
these PKC isoenzymes may play important roles in Ca2+/lipid-dependent
signal transduction and cell growth in these eukaryotes.