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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1997-2-21
|
| pubmed:abstractText |
Optimum conditions were determined for the solubilisation of native NMDA receptors of adult mammalian brain with the retention of [3H]MK-801 radioligand binding activity. The most efficient conditions were 1% Triton X-100/1 M NaCl. The efficiency of solubilisation was as follows: cloned NMDA receptors expressed in mammalian cells > forebrain receptors > cerebellar receptors. Triton X-100/1 M NaCl-solubilised forebrain NMDA receptors had a molecular size of 710,000 daltons, but significant NR1 immunoreactivity (41%) migrated as a monomer of 125,000 daltons. Immunoaffinity purification of NMDA receptors from forebrain by anti-NR1 911-920 antibody affinity chromatography from 1% Triton X-100/1 M NaCl solubilised extracts yielded purification of the NR1 Mr 120,000 immunoreactive species, but no detectable NR2A or NR2B immunoreactivity. Immunoprecipitation of NMDA receptors from Triton X-100/1 M NaCl extracts with anti-NR1 911-920 antibodies also resulted in precipitation of NR1 subunits, but with no detectable NR2A or NR2B subunits. In contrast, by immunoprecipitation with anti-NR1 17-35 antibodies, which recognise all forms of NR1, NR1, NR2A, and NR2B immunoreactivities were detected in the immune pellets. Similarly, a co-association of NR1, NR2A, and NR2B subunits was demonstrated following extraction of forebrain membranes with 1% sodium deoxycholate (pH 9) and purification by anti-NR1 911-920 antibody affinity chromatography. These results are consistent with the identification of a pool of unassembled C2 exon-containing NR1 subunits, i.e., NR1-1a, NR1-1b, NR1-2a, and NR1-2b, selectively solubilised by 1% Triton X-100/1 M NaCl.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0022-3042
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
68
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
507-16
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9003035-Age Factors,
pubmed-meshheading:9003035-Alternative Splicing,
pubmed-meshheading:9003035-Animals,
pubmed-meshheading:9003035-Antibody Specificity,
pubmed-meshheading:9003035-Cerebellum,
pubmed-meshheading:9003035-Chromatography, Affinity,
pubmed-meshheading:9003035-Chromatography, Gel,
pubmed-meshheading:9003035-Detergents,
pubmed-meshheading:9003035-Exons,
pubmed-meshheading:9003035-Gene Expression,
pubmed-meshheading:9003035-Humans,
pubmed-meshheading:9003035-Kidney,
pubmed-meshheading:9003035-Mice,
pubmed-meshheading:9003035-Molecular Weight,
pubmed-meshheading:9003035-Precipitin Tests,
pubmed-meshheading:9003035-Prosencephalon,
pubmed-meshheading:9003035-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:9003035-Solubility,
pubmed-meshheading:9003035-Transfection
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Biochemical evidence for the existence of a pool of unassembled C2 exon-containing NR1 subunits of the mammalian forebrain NMDA receptor.
|
| pubmed:affiliation |
Department of Pharmaceutical and Biological Chemistry, School of Pharmacy, London, England.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|