Unique uncoupling of the frog erythrocyte adenylate cyclase system by manganese. Loss of hormone and guanine nucleotide-sensitive enzyme activities without loss of nucleotide-sensitive, high affinity agonist binding.

@article{Limbird1979UniqueUO,
  title={Unique uncoupling of the frog erythrocyte adenylate cyclase system by manganese. Loss of hormone and guanine nucleotide-sensitive enzyme activities without loss of nucleotide-sensitive, high affinity agonist binding.},
  author={Lee E. Limbird and Aisling Hickey and Robert J Lefkowitz},
  journal={The Journal of biological chemistry},
  year={1979},
  volume={254 8},
  pages={2677-83}
}
Mn2+ at concentrations of -5 to 20 mu leads to a progressive loss of hormone (isoproterenol and prostaglandin El (PGEl)) and guanine nucleotide (Gpp(NH)p)-sensitive adenylate cyclase activity in frog erythrocyte membranes while basal and NaF activities remain relatively preserved. Mn2+ does not interfere with the recognition and binding of (-)-isoproterenol or PGEl at their specific receptors. In fact, despite the inability of Gpp(NH)p to stimulate adenylate cyclase in the presence of -20 mu… CONTINUE READING

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