Crystal structure of phlorizin and the iodothyronine deiodinase inhibitory activity of phloretin analogues.

@article{Aufmkolk1986CrystalSO,
  title={Crystal structure of phlorizin and the iodothyronine deiodinase inhibitory activity of phloretin analogues.},
  author={M Auf'mkolk and Josef Koehrle and Rolf D. Hesch and Sidney H Ingbar and Vivian Cody},
  journal={Biochemical pharmacology},
  year={1986},
  volume={35 13},
  pages={2221-7}
}
Phloretin, a 7,8-dihydrochalcone of plant origin, and the high molecular weight (less than 15,000) polyphloretinphosphate (PPP) polymers are potent inhibitors of iodothyronine monodeiodinase activity from rat liver microsomal preparations, whereas phlorizin, the 2'-O-glucoside of phloretin, is inactive. The polymers, differing in degree of phosphorylation-dependent polymerization, exhibited a concentration-dependent, and ultimately complete, inhibition of deiodinase activity with an IC50… CONTINUE READING
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