Identification and solubilization of atrial natriuretic factor receptors in human placenta.
Identification and solubilization of atrial natriuretic factor receptors in human placenta.
复制标题
人胎盘中心房钠尿因子受体的鉴定和溶解。
DOI：
10.1016/0006-291x(86)90019-7
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发表时间：
1986
影响因子：
3.1
通讯作者：
Sen,I
中科院分区：
文献类型：
--
作者：
Sen,I
特异性高亲和125i -心房钠素结合位点已在人胎盘膜中确定。使用非离子洗涤剂Triton X-100，定量地溶解这些结合位点并保持其结合活性。在溶解制剂中，结合心房利钠因子的大分子组分是一个160,000道尔顿蛋白，通过双功能化学交联剂二琥珀酰亚酸与125 -心房利钠因子共价交联，然后进行凝胶电泳和放射自显影。在Sephadex G-200凝胶过滤存在洗涤剂的情况下，洗脱出的激素受体复合物分子量在14万左右。这些观察结果有力地表明，人胎盘膜中存在的140-160,000道尔顿蛋白是特异性识别房钠因子的受体。
Specific high affinity125I-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 to125I-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.