Klotz K N, Lohse M J, Schwabe U
J Neurochem. 1986 May;46(5):1528-34. doi: 10.1111/j.1471-4159.1986.tb01772.x.
A1 adenosine receptors from rat brain membranes were solubilized with the zwitterionic detergent 3-[3-(cholamidopropyl)dimethylammonio]-1-propanesulfonate. The solubilized receptors retained all the characteristics of membrane-bound A1 adenosine receptors. A high and a low agonist affinity state for the radiolabelled agonist (R)-N6-[3H]phenylisopropyladenosine([3H]PIA) with KD values of 0.3 and 12 nM, respectively, were detected. High-affinity agonist binding was regulated by guanine nucleotides. In addition agonist binding was still modulated by divalent cations. The solubilized A1 adenosine receptors could be labelled not only with the agonist [3H]PIA but also with the antagonist 1,3-diethyl-8-[3H]phenylxanthine. Guanine nucleotides did not affect antagonist binding as reported for membrane-bound receptors. These results suggest that the solubilized receptors are still coupled to the guanine nucleotide binding protein Ni and that all regulatory functions are retained on solubilization.
用两性离子去污剂3-[3-(胆酰胺丙基)二甲基铵]-1-丙烷磺酸盐溶解大鼠脑膜中的A1腺苷受体。溶解后的受体保留了膜结合型A1腺苷受体的所有特性。检测到放射性标记激动剂(R)-N6-[3H]苯异丙基腺苷([3H]PIA)存在高亲和力和低亲和力激动剂结合状态，其KD值分别为0.3和12 nM。高亲和力激动剂结合受鸟嘌呤核苷酸调节。此外，激动剂结合仍受二价阳离子调节。溶解后的A1腺苷受体不仅可用激动剂[3H]PIA标记，也可用拮抗剂1,3-二乙基-8-[3H]苯基黄嘌呤标记。如膜结合型受体报道的那样，鸟嘌呤核苷酸不影响拮抗剂结合。这些结果表明，溶解后的受体仍与鸟嘌呤核苷酸结合蛋白Ni偶联，并且所有调节功能在溶解后得以保留。
