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KMID : 0380319920500000105
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Journal of Korean Research Institute for Better Living
1992 Volume.50 No. 0 p.105 ~ p.111
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Inhibition of the Adenylate Cyclase Activity by cAMP Dependent Protein Kinase
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Abstract
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To figure out possible roles of protein kinase A in the process of adenylate cyclase-desensitization, Ca^2+/calmodulin-sensitive adenylate cyclase was isolated from the membranes of lens fiber cells using calmodulin affinity column. The isolated adenylate cyclase which is free from GTP binding preteins, was gradually activated by various concentrations of calmodulin. However, the activity of adenylate cyclase was dramatically decreased in the presence of protein kinase A. Especially, stimulation of the activity of adenylate cyclase by calmodulin was almost abolished in the presence of protein kinase A. These results suggest that protein kinase A phosphorylates catalytic subunit of adenylate cyclase, and then inactivates enzyme activity.
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