G Protein .BETA..GAMMA.-Subunits Inhibit Purified Adenylate Cyclase Independent of the Activation by Ca2+ and Calmodulin.
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概要
- 論文の詳細を見る
Adenylate cyclase purified by affinity chromatography was activated about 2.5-fold in a Ca<SUP>2+</SUP>- and calmodulin-dependent fashion. G protein βγ-subunits, an inhibitor in the receptor-mediated inhibition of adenylate cyclase, inhibited the purified cyclase by more than 80%. The extent of βγ-induced inhibition was not affected by the activation with Ca<SUP>2+</SUP> and calmodulin. Moreover, the prior addition of the βγ-subunits to the cyclase did not prevent the subsequent activation of the enzyme by Ca<SUP>2+</SUP> and calmodulin. We conclude that the βγ-subunits inhibit adenylate cyclase activity in a calmodulin-independent mode.
- 公益社団法人 日本薬理学会の論文
著者
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Enomoto Keiichi
Department Of Environmental Systems Engineering Kochi University Of Technology
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Takano Masako
Department Of Pharmacology Faculty Of Medicine Saga Medical School
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ENOMOTO Keiichi
Department of Pharmacology, Saga Medical School
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ASAKAWA Takeo
Department of Pharmacology, Saga Medical School
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ASAKAWA Takeo
Department of Pharmacology I, Osaka University School of Medicine
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Hayama Kazuko
Department of Pharmacology, Saga Medical School
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- G Protein .BETA..GAMMA.-Subunits Inhibit Purified Adenylate Cyclase Independent of the Activation by Ca2+ and Calmodulin.