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Solubilization and partial characterization of adenosine binding sites from rat brainstem
Author(s) -
Nakata Hiroyasu,
Fujisawa Hitoshi
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)80683-8
Subject(s) - sodium cholate , chemistry , membrane , binding site , adenosine , chaps , solubilization , size exclusion chromatography , deoxycholic acid , sepharose , chromatography , biochemistry , biophysics , enzyme , biology , bile acid
Binding sites for adenosine were solubilized from rat brainstem membranes with either sodium cholate, sodium deoxycholate or 3‐[3‐cholamidopropyl)dimethyl‐ammonio]‐1‐propanesulfonate. About 30% of the binding activity were released by these detergents as assayed by [ 3 H]phenylisopropyladenosine (PIA) binding. Specific [ 3 H]PIA binding to the solubilized fraction was saturable and was found to be a monophasic saturation profile. In contrast, [ 3 H]PIA binding sites. By gel filtration on a Sepharose CL‐6B biphasic profile suggesting the presence of two binding sites. By gel filtration on a Sepharose CL‐6B column, the adenosine binding site—detergent complex was estimated to have app. M r 280 000 and r s = 5.4 nm.