In vivo regulation of hepatic protein kinase by adenosine 3',5'-monophosphate mediated glucagon stimulation |
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Authors: | O Sudilovsky |
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Institution: | Institute of Pathology, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, Ohio, USA |
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Abstract: | administration of glucagon caused an increase in the dissociation of protein kinase subunits which was accompanied by elevated adenosine 3′,5′-monophosphate concentrations in the rat liver. Concomitantly, there was a decrease in non saturated adenosine 3′,5′-monophosphate binding sites. A reduction in protein kinase activity measured in the presence of the cyclic nucleotide was apparent at 5 minutes of glucagon administration while enzyme activity assayed in the absence of adenosine 3′,5′-monophosphate was already increased after one minute. Glucose, given through an intragastric tube, caused no changes in the effect of glucagon on hepatic protein kinase. |
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