Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii
Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP puls protamine or histone. full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation...
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| Autores principales: | , , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_08986568_v2_n4_p395_Guthmann |
| Aporte de: |
| Sumario: | Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP puls protamine or histone. full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-riche histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3 fold the Vmax of kemptide phosphorylation by the ree catalytic subunits of both Mucor and bovine heart protein kinase; 10 μM polyarginine inhibited completely and activity of both enyzmes. © 1990. |
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