Two saturable recognition sites for (-) [125I]iodo-N6-(4-hydroxyphenyl-isopropyl)-adenosine binding on purified cardiac sarcolemma.

@article{Hausleithner1986TwoSR,
  title={Two saturable recognition sites for (-) [125I]iodo-N6-(4-hydroxyphenyl-isopropyl)-adenosine binding on purified cardiac sarcolemma.},
  author={Viktoria Hausleithner and Michael Freissmuth and Wolfgang Sch{\"u}tz},
  journal={Journal of receptor research},
  year={1986},
  volume={6 3-4},
  pages={311-21}
}
Analysis of (-) [125]iodo-N6-(4-hydroxyphenylisopropyl)-adenosine [( 125I]HPIA) binding to purified sarcolemmal preparations of guinea pig and bovine hearts revealed two classes of binding sites when unlabeled iodo-HPIA (100 mumol/l) was used as non-specific binding marker. In the presence of 1 mmol/l theophylline, however, only the high affinity component was detected. Adenosine receptor agonists caused biphasic displacement of [125I]HPIA binding, with a high affinity potency rank order… CONTINUE READING

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Biphasic competition curves were also observed with 8-phenyltheophylline and isobutylmethylxanthine , whereas the theophylline curve was monophasic up to 1 mmol / l .
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