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Molecular sizes of photolabeled GABA and benzodiazepine receptor proteins are identical
Author(s) -
Asano Tomiko,
Sakakibara Jinsaku,
Ogasawara Nobuaki
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80086-6
Subject(s) - muscimol , photoaffinity labeling , flunitrazepam , chemistry , gabaa receptor , receptor , benzodiazepine , biochemistry , polyacrylamide gel electrophoresis , membrane , gaba receptor , biophysics , biology , enzyme
[ 3 H]Muscimol was irreversibly incorporated into rat cerebellar membranes upon irradiation with ultraviolet light. GABA agonists and antagonists inhibited this incorporation. The reversible muscimolbinding decreased after photoaffinity‐labeling of the membranes with muscimol. These results indicated that this irreversible incorporation is to the GABA receptor. Photolabeled GABA receptor protein showed its M r of 50000±1000 in SDS—polyacrylamide gel electrophoresis. This molecular size is identical to that of the benzodiazepine receptor which was photolabeled with 3 H‐flunitrazepam.