Purification of ca2+/calmodulin-dependent protein kinase ii from rat stomach and its localization in the mucosa

Wei Jun Wang; Ko HJ1 Fukunaga; Satoshi Goto; Eishichi MIYAMoTo

doi:10.2220/biomedres.15.231

Purification of ca²⁺/calmodulin-dependent protein kinase ii from rat stomach and its localization in the mucosa

Wei Jun Wang, Ko HJ1 Fukunaga, Satoshi Goto, Eishichi MIYAMoTo

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Abstract

Ca²⁺/calmodulin-dependent protein kinase II (CaM kinase II) with a M_r 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.

Original language	English
Pages (from-to)	231-240
Number of pages	10
Journal	Biomedical Research (Japan)
Volume	15
Issue number	4
DOIs	https://doi.org/10.2220/biomedres.15.231
Publication status	Published - 1994
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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title = "Purification of ca2+/calmodulin-dependent protein kinase ii from rat stomach and its localization in the mucosa",

abstract = "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.",

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year = "1994",

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T1 - Purification of ca2+/calmodulin-dependent protein kinase ii from rat stomach and its localization in the mucosa

AU - Wang, Wei Jun

AU - Fukunaga, Ko HJ1

AU - Goto, Satoshi

AU - MIYAMoTo, Eishichi

PY - 1994

Y1 - 1994

N2 - 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.

AB - 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.

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Purification of ca²⁺/calmodulin-dependent protein kinase ii from rat stomach and its localization in the mucosa

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