N-Methyl--aspartate receptor channels are composed of an NR1 subunit and at least one of the NR2 subunits (NR2A-D). Activation of the N-methyl--aspartate receptor requires the coagonists glycine and glutamate. It has been proposed that the NR1 subunit possesses a glycine-binding site. We have expressed a soluble form of the NR1 subunit, which was produced by connecting the N-terminal extracellular region with the extracellular loop between the third and fourth membrane segments, by a baculovirus system along with full-length and truncated membrane-bound forms. The soluble NR1 receptor was efficiently secreted into the culture medium and showed a high affinity for ligands. The K d of a glycine-site antagonist, [$H]MDL 105,519[(E)-3-(2-phenyl-2-carboxyethenyl)-4,6-dichloro-1H-indole-2-carboxylic acid], for the soluble receptor was 3.89p0.97 nM, which was comparable to the K d of 4.47p1.39 nM for the membrane-bound full-length form. These values were close to the values reported previously with the use
Three isomers of [Co3(edma)3(μ-OH)3(μ3-O)]+ (edma: ethylenediamine-N-acetate) containing a partial cubane Co3O4 core were prepared and the structure of one of the isomers was determined by the X-ray diffraction method. These isomers are stable at least for 5 days in their neutral aqueous solutions.
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