Hamada M, Rondon I J, Frohlich E D, Cole F E
Biochem Biophys Res Commun. 1987 May 29;145(1):257-62. doi: 10.1016/0006-291x(87)91314-3.
The elution profile of solubilized rat glomerular membranes from a gel filtration column showed two peaks of 125I-ANF (atrial natriuretic factor) binding (367 +/- 21, 156 +/- 12 KDa). Over 85% of the total binding for the extract was in the 367 KDa peak. Guanylate cyclase activity was correlated with 125I-ANF specific binding. ANF activation of guanylate cyclase was also observed. As observed previously with particulate membrane, Scatchard-analysis of ANF binding data with the solubilized extract was consistent with a two-site model. Both affinities (Kd's), 4 pM and 1 nM, are within the range of blood concentrations reported for ANF. These observations suggest that most rat glomerular ANF receptors are large molecular complexes coupled with guanylate cyclase in the 300-350 KDa size range.
来自凝胶过滤柱的溶解大鼠肾小球膜的洗脱图谱显示出两个125I-心房钠尿肽（ANF）结合峰（367 +/- 21、156 +/- 12千道尔顿）。提取物总结合量的85%以上位于367千道尔顿峰中。鸟苷酸环化酶活性与125I-ANF特异性结合相关。还观察到ANF对鸟苷酸环化酶的激活作用。如先前在微粒膜中所观察到的，用溶解提取物对ANF结合数据进行Scatchard分析与双位点模型一致。两种亲和力（解离常数），4皮摩尔和1纳摩尔，均在报道的ANF血浓度范围内。这些观察结果表明，大多数大鼠肾小球ANF受体是与300 - 350千道尔顿大小范围内的鸟苷酸环化酶偶联的大分子复合物。
