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Regulation of intracellular cyclic amp binding to membranes in human erythrocytes


, : Regulation of intracellular cyclic amp binding to membranes in human erythrocytes. Agricultural & Biological Chemistry 51(4): 1033-1038

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.

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Related references

Tsukamoto, T.; Yamakawa, Y.; Inaba, T., 1987: Regulation of intracellular cAMP binding to membranes in human erythrocytes. Agricultural and Biological Chemistry 51: 33-7

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