Rugg E L, Aiton J F, Cramb G
Department of Biology and Preclinical Medicine, University of St. Andrews, Fife, UK.
Biochem Biophys Res Commun. 1989 Aug 15;162(3):1339-45. doi: 10.1016/0006-291x(89)90820-6.
Two classes of atrial natriuretic peptide (ANP) receptors are present in purified sarcolemmal membrane fractions isolated from rat ventricle. Scatchard analysis using [125I]-ANP reveals high affinity (Kd approximately 10(-11) M) and low affinity (Kd approximately 10(-9) M) binding sites. Basal guanylate cyclase activities associated with these membrane fractions range from 3.2 +/- 1.3 pmol/min/mg protein in the presence of Mg2+ to 129 +/- 17 pmol/min/mg protein in the presence of Mn2+. Millimolar concentrations of adenosine triphosphate (ATP) potentiates Mg2+- but not Mn2+-supported activity. Binding of ANP to the low affinity site but not the high affinity site results in a maximum 2-fold activation of Mn2+- and up to 6-fold activation of Mg2+/ATP supported guanylate cyclase activities.
从大鼠心室分离得到的纯化肌膜组分中存在两类心房利钠肽（ANP）受体。使用[125I]-ANP进行的Scatchard分析显示出高亲和力（Kd约为10^(-11) M）和低亲和力（Kd约为10^(-9) M）结合位点。与这些膜组分相关的基础鸟苷酸环化酶活性在存在Mg2+时为3.2±1.3 pmol/分钟/毫克蛋白质，在存在Mn2+时为129±17 pmol/分钟/毫克蛋白质。毫摩尔浓度的三磷酸腺苷（ATP）增强了Mg2+支持的活性，但不增强Mn2+支持的活性。ANP与低亲和力位点而非高亲和力位点的结合导致Mn2+支持的鸟苷酸环化酶活性最大激活2倍，Mg2+/ATP支持的鸟苷酸环化酶活性最大激活6倍。
