Carrier F, Thibault G, Schiffrin E L, Garcia R, Gutkowska J, Cantin M, Genest J
Biochem Biophys Res Commun. 1985 Oct 30;132(2):666-73. doi: 10.1016/0006-291x(85)91184-2.
Specific receptors for atrial natriuretic factor (ANF) have been identified and solubilized in glomeruli from rat kidney. Radioiodinated synthetic ANF (Arg 101-Tyr 126) bound to a single class of high affinity (Kd 27 +/- 24 pM) sites with a density of 390 +/- 230 fmole/mg protein. The binding was time- and temperature-dependent, saturable and reversible. The ANF-receptor complex was not affected by angiotensin II, ACTH or vasopressin. Solubilization with 10 mM 3-[(3-cholamidopropyl)-dimethylammonio]- 1-propane sulfonate (CHAPS) slightly increased the affinity for ANF (Kd 5.0 +/- 3.3 pM) without affecting the density (250 +/- 110 fmole/mg protein). Similar results were found with 1% Triton X-100. ANF-related peptides interact generally in the same way with non-solubilized and solubilized receptors, indicating a fully preserved specificity of the receptors.
心房利钠因子（ANF）的特异性受体已在大鼠肾脏肾小球中被鉴定并溶解。放射性碘化合成ANF（精氨酸101 - 酪氨酸126）与一类高亲和力（解离常数Kd为27±24皮摩尔）位点结合，其密度为390±230飞摩尔/毫克蛋白质。这种结合具有时间和温度依赖性、可饱和性和可逆性。ANF受体复合物不受血管紧张素II、促肾上腺皮质激素或加压素的影响。用10毫摩尔3 - [（3 - 胆酰胺丙基） - 二甲基铵] - 1 - 丙烷磺酸盐（CHAPS）溶解可略微增加对ANF的亲和力（Kd为5.0±3.3皮摩尔），而不影响其密度（250±110飞摩尔/毫克蛋白质）。用1% Triton X - 100也得到了类似结果。ANF相关肽与未溶解和已溶解的受体通常以相同方式相互作用，表明受体的特异性完全保留。
