Effect of polyanions and polycations on adenosine 3',5'-monophosphate-binding and protein kinase activity. |
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Authors: | M Shimoyama M Kawai S Yamamoto H Imai A Kitamura |
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Affiliation: | Department of Medical Chemistry, Osaka Medical College, Takatsuki, Osaka, Japan |
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Abstract: | Histone, protamine, poly-L-arginine, and poly-L-lysine enhance the binding of adenosine 3′,5′-monophosphate (cyclic AMP) to rat liver cyclic AMP-dependent protein kinase as determined by Millipore filtration assay. Poly-L-glutamic acid and poly-L-aspartic acid suppress cyclic AMP-binding stimulated by histone. Poly-L-glutamic acid and poly-L-aspartic acid are effective against protein kinase and result in decrease in initial reaction velocity when histone is used as a protein substrate. Incubation of cyclic AMP-dependent protein kinase with 6 μg poly-L-glutamic acid produces half-maximal inhibition of cyclic AMP-dependent protein kinase when 30 μg histone is used as substrate. |
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