Linked Life Data

8843152

Source:http://linkedlifedata.com/resource/pubmed/id/8843152

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pubmed-article:8843152pubmed:abstractTextThe functional reconstitution of glutamate receptor proteins purified from mammalian brain has been difficult to accomplish. However, channels activated by L-glutamate (L-Glu) and N-methyl-D-aspartate (NMDA) were detected in planar lipid bilayer membranes (PLMs) following the reconstitution of a complex of proteins with binding sites for NMDA receptor (NMDAR) ligands. The presence of glycine was necessary for optimal activation. A linear current-voltage relationship was observed with the reversal potential being zero. Channels activated by L-Glu had conductances of 23, 47 and 65 pS, and were suppressed partially by competitive and fully by noncompetitive inhibitors of NMDARs. Magnesium had little effect on the reconstituted channels.lld:pubmed
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pubmed-article:8843152pubmed:articleTitleIon channel properties of a protein complex with characteristics of a glutamate/N-methyl-D-aspartate receptor.lld:pubmed
pubmed-article:8843152pubmed:affiliationDepartment of Biochemistry, Center for Neurobiology and Immunology Research, University of Kansas, Lawrence 66045, USA.lld:pubmed
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pubmed-article:8843152pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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