Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) with a Mr of 530,000 was purified from rat stomach. The enzyme showed a major protein band with 52 kDa and minor components with 50 and 54 kDa when examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The physicochemical and kinetic properties of the enzyme were similar to those of brain CaM kinase II. The enzyme showed a broad substrate specificity, and wascapable of phosphorylating several endogenous proteins in the cytosol and membrane fractions.The polyclonal antibody against brain CaM kinase II cross-reacted with the enzyme.Strong immunoreactivity was observed in the parietal cells of stomach by the immunohistochemical investigation. These results suggest that CaM kinase II regulates the Ca2+-dependent cellular functions of the parietal cells.
|Number of pages||10|
|Journal||Biomedical Research (Japan)|
|Publication status||Published - 1994|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)