Purification and subunit composition of atrial natriuretic peptide receptor.
Purification and subunit composition of atrial natriuretic peptide receptor.
复制标题
心房钠尿肽受体的纯化和亚基组成。
DOI：
--
复制
发表时间：
1987
影响因子：
11.1
通讯作者：
J. Lewicki
中科院分区：
文献类型：
--
作者：
D. Schenk;M. Phelps;J. G. Porter;F. Fuller;B. Cordell;J. Lewicki
用亲和层析法从培养的牛主动脉平滑肌细胞中纯化了心房利钠肽（ANP）受体，纯化倍数为2700倍。通过metrizamide梯度离心和非还原NaDodSO 4/聚丙烯酰胺凝胶电泳测定，天然ANP受体的分子量为125，000。以~（125）I标记的心钠素为配体，纯化的心钠素受体的最大结合量为5.70nmol/mg蛋白，解离常数为4.0 × 10 ~（-10）M。在用10 mM二硫苏糖醇处理后，纯化的受体在NaDodSO 4/聚丙烯酰胺凝胶电泳中迁移为Mr 60，500的单一条带。这些发现表明，血管组织中ANP的全受体由两个表观分子量相同的亚基组成，推测由二硫桥连接。
A receptor for atrial natriuretic peptide (ANP) was purified 2700-fold, to apparent homogeneity, from cultured bovine aortic smooth muscle cells by affinity chromatography. The native ANP receptor has a molecular weight of 125,000 as determined by both metrizamide gradient centrifugation and nonreducing NaDodSO4/polyacrylamide gel electrophoresis. With 125I-labeled ANP as ligand, the purified receptor bound a maximum of 5.70 nmol of ligand per mg of protein and the dissociation constant was 4.0 X 10(-10)M. Upon treatment with 10 mM dithiothreitol, the purified receptor migrated as a single band at Mr 60,500 in NaDodSO4/polyacrylamide gel electrophoresis. These findings show that the holoreceptor for ANP in vascular tissue is composed of two subunits of identical apparent molecular weight, presumably linked by a disulfide bridge(s).