Schenk D B, Phelps M N, Porter J G, Scarborough R M, McEnroe G A, Lewicki J A
J Biol Chem. 1985 Dec 5;260(28):14887-90.
Binding experiments with 125I-atrial natriuretic factor (ANF) followed by covalent attachment with disuccimidyl suberate show that the peptide binds predominantly to a protein of apparent molecular mass of 66,000 daltons on the cell surface of cultured bovine aortic smooth muscle cells. A minor protein species of 180,000 Mr is also visualized after cross-linking. Endothelial cells, however, whose ANF binding parameters differ substantially from smooth muscle cells, also appear to have qualitatively identical 125I-ANF binding proteins. The identity of these putative proteins, as the ANF receptor, is confirmed by findings that covalent attachment of 125I-ANF is saturable, concentration-dependent, and competed by nanomolar concentrations of unlabeled ANF. Furthermore, other peptide hormones such as angiotensin II, glucagon, or insulin are ineffective in competing for 125I-ANF binding and cross-linking to the receptor.
用125I-心房利钠因子（ANF）进行结合实验，随后用辛二酸二琥珀酰亚胺酯进行共价连接，结果表明该肽主要结合于培养的牛主动脉平滑肌细胞表面一种表观分子量为66,000道尔顿的蛋白质。交联后还可见到一种分子量为180,000的次要蛋白质。然而，内皮细胞的ANF结合参数与平滑肌细胞有很大差异，但其125I-ANF结合蛋白在性质上似乎也相同。这些假定蛋白质作为ANF受体的身份通过以下发现得以证实：125I-ANF的共价连接是可饱和的、浓度依赖性的，并被纳摩尔浓度的未标记ANF所竞争。此外，其他肽类激素如血管紧张素II、胰高血糖素或胰岛素在竞争125I-ANF与受体的结合和交联方面无效。
