Activation Mechanism of Protein Kinases from Rat Tissues by Adenosine 3', 5'-Monophosphate

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概要

• 論文の詳細を見る

• 3', 5'-Cyclic AMP (cyclic AMP)-dependent and independent protein kinases (protein kinase B<SUB>1</SUB> and B<SUB>2</SUB>, respectively) and a cyclic AMP-binding protein (R-protein) are partially purified from rat liver. Although R-protein shows no kinase activity, it almost totally depresses protein kinase B<SUB>2</SUB> activity. Cyclic AMP relieves the kinase of the inhibition by R-protein. The treatment of protein kinase B<SUB>1</SUB> with cyclic AMP resolves the kinase into R-protein and protein kinase B<SUB>2</SUB>. The evidence indicates that protein kinase B<SUB>1</SUB> is a complex of R-protein and protein kinase B<SUB>2</SUB>, and that cyclic AMP may regulate the attachment of R-protein to the protein kinase.

• Japan Society of Clinical Chemistryの論文

著者

• 山村 博平

  神戸大学医学部第1生化学講座

• 武田 誠郎

  神戸大学医学部第二生化学

• 公文 明

  神戸大学医学部第二生化学

関連論文

• 女医さん (トピックス 女医問題II)
• 神戸大学医学部第一生化学講座 (教室だより)
• Amplification of Hormone Action by Adenosine 3', 5'-onophosphate-Dependent Protein Kinase
• Activation Mechanism of Protein Kinases from Rat Tissues by Adenosine 3', 5'-Monophosphate

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