Chazot P L, Cik M, Stephenson F A
Department of Pharmaceutical Chemistry, School of Pharmacy, University of London, England.
J Neurochem. 1992 Sep;59(3):1176-8. doi: 10.1111/j.1471-4159.1992.tb08364.x.
The rat NMDAR1 (N-methyl-D-aspartate receptor) was expressed transiently in human embryonic kidney cells. Transfected cell homogenates showed saturable [3H]MK-801 binding activity that was best fit by a single high-affinity site with a KD of 9 nM and a Bmax of 113 fmol of binding sites/mg of protein. Antibodies raised against the peptide sequence NMDAR1 (929-938) coupled to keyhole limpet haemocyanin specifically recognised a single band with M(r) 117,000 in immunoblots from adult rat brain. In the transfected cells, the antibody recognised two bands: one with M(r) 117,000, which was coincident with that from brain membranes, and one with M(r) 97,000, which was identified as nonglycosylated NMDAR1 subunit. These results identify the NMDAR1 of rat brain and further show that the homooligomer binds MK-801, albeit at low efficiency.
大鼠NMDAR1（N-甲基-D-天冬氨酸受体）在人胚肾细胞中瞬时表达。转染细胞匀浆显示出可饱和的[3H]MK-801结合活性，该活性最适合由一个KD为9 nM、Bmax为113 fmol结合位点/毫克蛋白质的单一高亲和力位点来描述。针对与钥孔血蓝蛋白偶联的肽序列NMDAR1（929 - 938）产生的抗体在成年大鼠脑免疫印迹中特异性识别出一条分子量为117,000的条带。在转染细胞中，该抗体识别出两条带：一条分子量为117,000，与脑膜中的条带一致；另一条分子量为97,000，被鉴定为非糖基化的NMDAR1亚基。这些结果鉴定了大鼠脑的NMDAR1，并进一步表明同源寡聚体结合MK-801，尽管效率较低。
