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

薬学研究科・生命薬科学専攻

研究成果: Article › 査読

1 被引用数 (Scopus)

抄録

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.

本文言語	English
ページ（範囲）	231-240
ページ数	10
ジャーナル	Biomedical Research (Japan)
巻	15
号	4
DOI	https://doi.org/10.2220/biomedres.15.231
出版ステータス	Published - 1994

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

文献へのアクセス

10.2220/biomedres.15.231

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引用スタイル

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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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AU - Wang, Wei Jun

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AU - MIYAMoTo, Eishichi

PY - 1994

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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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