Sen I
Biochem Biophys Res Commun. 1986 Mar 13;135(2):480-6. doi: 10.1016/0006-291x(86)90019-7.
Specific high affinity 125I-atrial natriuretic factor binding sites have been identified in human placental membranes. Using the nonionic detergent, Triton X-100, these binding sites were quantitatively solubilized and retained binding activity. In the solubilized preparation, the macromolecular component that binds atrial natriuretic factor is a 160,000 dalton protein as shown by covalently cross-linking it to 125I-atrial natriuretic factor with the bifunctional chemical crosslinker, disuccinimidyl suberate, followed by gel electrophoresis and autoradiography. On Sephadex G-200 gel filtration in the presence of detergent, the hormone-receptor complex elutes in the molecular weight range of 140,000. These observations suggest strongly that a 140- 160,000 dalton protein present in human placental membranes is the receptor for specific recognition of atrial natriuretic factor.
在人胎盘膜中已鉴定出特异性高亲和力的125I - 心房利钠因子结合位点。使用非离子去污剂Triton X - 100，这些结合位点被定量溶解并保留结合活性。在溶解的制剂中，通过用双功能化学交联剂辛二酸二琥珀酰亚胺酯将其与125I - 心房利钠因子共价交联，然后进行凝胶电泳和放射自显影，显示与心房利钠因子结合的大分子成分是一种160,000道尔顿的蛋白质。在去污剂存在下进行Sephadex G - 200凝胶过滤时，激素 - 受体复合物在分子量范围为140,000处洗脱。这些观察结果强烈表明，人胎盘膜中存在的140 - 160,000道尔顿蛋白质是特异性识别心房利钠因子的受体。
