Characterization of [3H]Ouabain Binding Sites in Human Brain, Platelet, and Erythrocyte

R. Hauger, H. M.D. Luu, F. K. Goodwin, S. M. Paul

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[3H]Ouabain binding was investigated in membranes prepared from human brain, erythrocyte, and platelet. Scatchard analysis of [3H]ouabain binding to human hypothalamic membranes revealed a single class of noninteracting binding sites with an apparent affinity constant (KD) of 21 nM. Though the number of [3H]ouabain binding sites was lower in human platelets than in erythrocytes, both tissues exhibited a single class of high‐affinity binding sites with an apparent KD similar to that found in human brain. Specific [3H]ouabain binding in basal ganglia tissue from patients with Huntington's disease was more than 50% lower than in tissue from age‐ and sex‐matched controls. These results, along with previous findings in rat brain, suggest that high‐affinity [3H]ouabain binding labels the neuronal form of Na,K‐ATPase in human brain, and may prove useful in quantitating this enzyme in postmortem brain samples.

Original languageEnglish
Pages (from-to)1704-1708
Number of pages5
JournalJournal of Neurochemistry
Issue number6
StatePublished - Jun 1985


  • Central nervous system
  • Huntington's disease
  • Na,K‐ATPase
  • Ouabain


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