pubmed-article:2825805 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2825805 | lifeskim:mentions | umls-concept:C0018038 | lld:lifeskim |
pubmed-article:2825805 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
pubmed-article:2825805 | lifeskim:mentions | umls-concept:C0064219 | lld:lifeskim |
pubmed-article:2825805 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:2825805 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2825805 | pubmed:dateCreated | 1988-2-11 | lld:pubmed |
pubmed-article:2825805 | pubmed:abstractText | The binding of [3H]kainate to goldfish brain membrane fragments was investigated. Scatchard analysis revealed a single class of binding sites in Tris-HCl buffer with a Kd of 352 nM and a Bmax of 3.1 pmol/mg wet weight. In Ringer's saline, [3H]kainate bound with a Bmax of 1.8 pmol/mg wet weight and a Kd of 214 nM. Binding in Ringer's saline, but not Tris-HCl buffer, displayed positive cooperativity with a Hill coefficient of 1.15. The [3H]kainate binding sites were solubilized in Ringer's saline using the nonionic detergent n-octyl-beta-D-glucopyranoside. Approximately 30-50% of the total number of membrane-bound binding sites were recovered on solubilization. The Kd of [3H]kainate for solubilized binding sites was approximately 200 nM. The rank order of potency for glutamatergic ligands at inhibiting [3H]kainate binding was identical and the competitive ligands had similar Ki values in both membranes and solubilized extracts. In membrane preparations, [3H]kainate displayed a two component off-rate with koff values of 0.97 min-1 and 0.07 min-1; in solubilized extracts, however, only a single off-rate (koff = 0.52 min-1) was observed. The hydrodynamic properties of n-octyl-beta-D-glucopyranoside solubilized [3H]kainate binding sites was investigated by sucrose density centrifugation. A single well defined peak was detected which yielded a sedimentation coefficient of 8.3 S. The results presented in this report suggest that goldfish brain may provide an ideal system in which to study kainate receptor biochemistry. | lld:pubmed |
pubmed-article:2825805 | pubmed:language | eng | lld:pubmed |
pubmed-article:2825805 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2825805 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2825805 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2825805 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2825805 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2825805 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2825805 | pubmed:month | Jan | lld:pubmed |
pubmed-article:2825805 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:2825805 | pubmed:author | pubmed-author:OswaldR ERE | lld:pubmed |
pubmed-article:2825805 | pubmed:author | pubmed-author:HenleyJ MJM | lld:pubmed |
pubmed-article:2825805 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2825805 | pubmed:day | 13 | lld:pubmed |
pubmed-article:2825805 | pubmed:volume | 937 | lld:pubmed |
pubmed-article:2825805 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2825805 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2825805 | pubmed:pagination | 103-11 | lld:pubmed |
pubmed-article:2825805 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:2825805 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:2825805 | pubmed:articleTitle | Solubilization and characterization of kainate receptors from goldfish brain. | lld:pubmed |
pubmed-article:2825805 | pubmed:affiliation | Department of Pharmacology, New York State College of Veterinary Medicine, Cornell University, Ithaca 14853-6401. | lld:pubmed |
pubmed-article:2825805 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2825805 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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