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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1982-7-19
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pubmed:abstractText |
[3H]Muscimol and [3H]flunitrazepam binding activities have been solubilized from bovine cortex using the ionic detergent sodium deoxycholate. The soluble receptor proteins were shown to bind [3H]muscimol with a dissociation constant, Kd, of 12 nM and a binding capacity (Bmax value) of 1.56 pmol/mg protein; gamma-amino[3H]-butyric acid with a Kd of 50 nM and Bmax of 1.55 pmol/mg protein; and [3H]flunitrazepam with a Kd of 8 nM and a Bmax of 0.8 pmol/mg protein. Gel filtration of the soluble receptor proteins showed that the gamma-amino[3H]butyric acid and [3H]flunitrazepam binding activities comigrated with a Stokes radius of 6.8 nm. The two binding activities were also found to comigrate after sedimentation in a sucrose density gradient. The hydrodynamic properties of the assumed protein-detergent complexes were determined by gel filtration and sedimentation through gradients of sucrose in H2O or 2H2O. Under the conditions employed, the parameters for both the putative gamma-aminobutyric acid and benzodiazepine receptors were: partial specific volume, 0.73 ml g-1; sedimentation coefficient, 12.5 S; molecular weight, 355000; and frictional ratio 1.46. These observations are consistent with the conclusion that the majority of both binding activities solubilized in deoxycholate reside in a single macromolecular complex. However, Triton X-100 selectively solubilized the benzodiazepine binding activity. This suggests that the two binding activities can be at least partially separated.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Deoxycholic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Flunitrazepam,
http://linkedlifedata.com/resource/pubmed/chemical/Muscimol,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Drug,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, GABA-A,
http://linkedlifedata.com/resource/pubmed/chemical/gamma-Aminobutyric Acid
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
123
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
291-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6281005-Animals,
pubmed-meshheading:6281005-Cattle,
pubmed-meshheading:6281005-Centrifugation, Density Gradient,
pubmed-meshheading:6281005-Cerebral Cortex,
pubmed-meshheading:6281005-Chemistry, Physical,
pubmed-meshheading:6281005-Chromatography, Gel,
pubmed-meshheading:6281005-Deoxycholic Acid,
pubmed-meshheading:6281005-Flunitrazepam,
pubmed-meshheading:6281005-Molecular Weight,
pubmed-meshheading:6281005-Muscimol,
pubmed-meshheading:6281005-Physicochemical Phenomena,
pubmed-meshheading:6281005-Receptors, Cell Surface,
pubmed-meshheading:6281005-Receptors, Drug,
pubmed-meshheading:6281005-Receptors, GABA-A,
pubmed-meshheading:6281005-Solubility,
pubmed-meshheading:6281005-gamma-Aminobutyric Acid
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pubmed:year |
1982
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pubmed:articleTitle |
Physicochemical characterization of detergent-solubilized gamma-aminobutyric acid and benzodiazepine receptor proteins from bovine brain.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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