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Characterization of [ 3 H]Ouabain Binding Sites in Human Brain, Platelet, and Erythrocyte
Author(s) -
Hauger R.,
Luu H. M. D.,
Goodwin F. K.,
Paul S. M.
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb07157.x
Subject(s) - ouabain , human brain , platelet , binding site , basal (medicine) , medicine , membrane , endocrinology , enzyme , brain tissue , biochemistry , biology , chemistry , microbiology and biotechnology , neuroscience , sodium , organic chemistry , insulin
[ 3 H]Ouabain binding was investigated in membranes prepared from human brain, erythrocyte, and platelet. Scatchard analysis of [ 3 H]ouabain binding to human hypothalamic membranes revealed a single class of noninteracting binding sites with an apparent affinity constant ( K D ) of 21 n M. Though the number of [ 3 H]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 K D similar to that found in human brain. Specific [ 3 H]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 [ 3 H]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.