Rapidly reversible binding of rabbit prolactin to the rabbit prolactin receptor accounts for the differences between homologous and heterologous binding.

@article{Ptridou1997RapidlyRB,
  title={Rapidly reversible binding of rabbit prolactin to the rabbit prolactin receptor accounts for the differences between homologous and heterologous binding.},
  author={Barbara P{\'e}tridou and Claire Cahoreau and Jean Djiane},
  journal={The Journal of endocrinology},
  year={1997},
  volume={153 2},
  pages={207-19}
}
The binding of radioiodinated rabbit (rb) prolactin (PRL) to rabbit mammary membranes is low and its affinity constant, 0.02 nM-1, calculated from heterologous inhibition assays, is about 300 times lower than that of ovine (o) PRL. Although the differences between homologous and heterologous binding are well documented in different species, the reasons for such differences are still unknown. Here we show that the low affinity of rbPRL for the native receptor does not affect its in vitro… CONTINUE READING

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