Vandlen R L, Arcuri K E, Hupe L, Keegan M E, Napier M A
Fed Proc. 1986 Aug;45(9):2366-70.
Specific, high-affinity receptors for atrial natriuretic factor (ANF) have been identified on membranes from a variety of tissues and cultured cells. By affinity labeling procedures, radioactivity from 125I-labeled ANF was specifically incorporated into three different polypeptides of ca. 120,000, 70,000, and 60,000 daltons, which may represent the binding subunits of ANF receptors. These polypeptides were present in varying amounts in different target tissues. In rat adrenal membranes, the 120,000- and 70,000-dalton peptides were specifically labeled whereas in A10 rat smooth muscle cells, only the 60,000-dalton peptide was labeled. Membranes from rat kidney and rabbit aorta contain all three peptides. Gel filtration chromatography of solubilized receptors suggested that intact ANF receptors are large molecular complexes with apparent molecular masses in the range of 250,000-350,000 daltons. The differential labeling pattern observed with the various tissues suggested that there might be at least two different receptors composed of unique ANF-binding polypeptides.
在多种组织和培养细胞的膜上已鉴定出心房利钠因子（ANF）的特异性、高亲和力受体。通过亲和标记程序，125I标记的ANF的放射性被特异性地掺入到三种不同的多肽中，其分子量约为120,000、70,000和60,000道尔顿，这可能代表ANF受体的结合亚基。这些多肽在不同的靶组织中的含量各不相同。在大鼠肾上腺膜中，120,000道尔顿和70,000道尔顿的肽被特异性标记，而在A10大鼠平滑肌细胞中，只有60,000道尔顿的肽被标记。大鼠肾脏和兔主动脉的膜含有所有三种肽。对溶解的受体进行凝胶过滤层析表明，完整的ANF受体是大分子复合物，其表观分子量在250,000 - 350,000道尔顿范围内。在各种组织中观察到的差异标记模式表明，可能至少存在两种由独特的ANF结合多肽组成的不同受体。
