Re-evaluation of the specificity of adenylyl (beta,gamma-methylene)diphosphonate as a substrate for adenylate cyclase.

@article{Mayer1991ReevaluationOT,
  title={Re-evaluation of the specificity of adenylyl (beta,gamma-methylene)diphosphonate as a substrate for adenylate cyclase.},
  author={Doris Mayer and Hans Hacker and Peter Bannasch},
  journal={The Histochemical journal},
  year={1991},
  volume={23 2},
  pages={100-6}
}
The conversion of the ATP-analogue adenylyl(beta,gamma-methylene)diphosphonate (AMPPCP) to cyclic AMP by adenylate cyclase of rat liver membranes was demonstrated using a radioimmunoassay for cyclic AMP. The conversion was only insignificantly lower than with adenylylimidodiphosphate (AMPPNP), another ATP-analogue which is usually used in the histochemical adenylate cyclase assay. The unspecific phosphate production was lower with AMPPCP as compared to AMPPNP. Therefore AMPPCP is considered to… CONTINUE READING