A cAMP receptor from mouse liver cytosol whose binding capacity is enhanced by Mg++-ATP. |
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Authors: | S O Doskeland P M Ueland |
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Institution: | Cell Biology Research Group, Department of Anatomy University of Bergen, Bergen, Norway |
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Abstract: | A receptor with a dissociation constant of 2·10?6M for cyclic 3′,5′-AMP (cAMP) has been found in mouse liver cytosol. This cAMP binding activity can be differentiated from the cAMP-dependent protein kinase holoenzymes and the free regulatory subunits also found in the cytosol. Mg++-ATP increases the number of binding sites for cAMP several fold. This increased capacity for cAMP binding persists after Sephadex G-25 filtration, and incubation for 14 hours in the presence of 5 mM EDTA. Among several adenosine- and guanosine-derivatives tested, only AMP, ADP and ATP compete efficiently with 3H] cAMP for the cAMP binding site. |
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