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Regulation of intracellular cyclic amp binding to membranes in human erythrocytes


Agricultural & Biological Chemistry 51(4): 1033-1038
Regulation of intracellular cyclic amp binding to membranes in human erythrocytes
The intracellular factors which may regulate cAMP binding to the inner surface of membranes in human erythrocytes were investigated. [3H]cAMP binding studies on isolated membranes at 30.degree. C in the presence of plausible cAMP binding regulators such as proteins, nucleosides, and non-cyclic nucleotides suggested that ATP could be the most potent regulator of cAMP binding to human erythrocyte membranes. ATP inhibition of [3H]cAMP binding to human erythrocyte membranes was competitive and temperature-dependent. The apparent dissociation constant for the cAMP-membrane complex was 10 nM at 30.degree. C in the absence of ATP. The presence of 1 mM ATP increased the constant to 63 nM.


Accession: 006288855



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