Abstract
Adenosine 3':5' cyclic monophosphate (cyclic AMP) binds to proteins present in the 100,000 g supernatant fractions of full-grown oocytes of Xenopus laevis. Optimal pH for the binding is 4.0. Two receptor binding sites have been characterized by density gradient centrifugation as peaks with sedimentation constants of 4.6 S and 5.9 S. The apparent dissociation constants for the two cyclic AMP binding sites are 7 nM and 40 nM. The total cyclic AMP binding capacity of oocyte cytosol is 15.8 +/- 2.2 fmoles/oocyte and remains constant during meiotic maturation induced by progesterone.
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