Hirose S, Akiyama F, Shinjo M, Ohno H, Murakami K
Biochem Biophys Res Commun. 1985 Jul 31;130(2):574-9. doi: 10.1016/0006-291x(85)90455-3.
Receptors for atrial natriuretic factor (ANF) have been solubilized with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate from bovine adrenal cortex and characterized. The detergent extract retained specific high-affinity binding sites for 125I-ANF. Scatchard analysis of the equilibrium binding data revealed a single class of binding site with a K-d of 1.8 nM and a maximum binding capacity of 2.5 pmol/mg of protein. The size of the 125I-ANF X receptor complexes was estimated to be 140,000 daltons by gel filtration on TSK gel G3000SW. Affinity labeling followed by electrophoresis under nonreducing conditions and autoradiography also revealed a single band of a similar size (Mr = 130,000); this band, however, migrated as a Mr = 70,000 species under reducing electrophoretic conditions. These results indicate that the ANF receptor, having a Mr of 130,000 - 140,000, is composed of disulfide-linked subunits and the ANF-binding site is located on the 70-kDa component.
心房利钠因子（ANF）受体已用3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸盐从牛肾上腺皮质中溶解并进行了表征。去污剂提取物保留了对125I-ANF的特异性高亲和力结合位点。对平衡结合数据的Scatchard分析显示有一类结合位点，解离常数（K-d）为1.8 nM，最大结合容量为2.5 pmol/mg蛋白质。通过在TSK凝胶G3000SW上进行凝胶过滤，估计125I-ANF与受体复合物的大小为140,000道尔顿。亲和标记后在非还原条件下进行电泳和放射自显影，也显示出一条大小相似的单带（Mr = 130,000）；然而，在还原电泳条件下，这条带迁移为Mr = 70,000的条带。这些结果表明，Mr为130,000 - 140,000的ANF受体由二硫键连接的亚基组成，且ANF结合位点位于70 kDa的组分上。
