猪肺中降钙素特异性受体的特性研究
Characterization of specific receptors for calcitonin in porcine lung.
作者信息
Fouchereau-Peron M, Moukhtar M S, Benson A A, Milhaud G
出版信息
Proc Natl Acad Sci U S A. 1981 Jun;78(6):3973-5. doi: 10.1073/pnas.78.6.3973.
The binding of salmon calcitonin was investigated in subcellular fractions obtained from normal porcine lung. Only the membrane fraction (density, 1.14 g/cm3) showed specific binding for calcitonin. Specific binding of 125I-labeled salmon calcitonin was competitively inhibited by concentrations of unlabeled homologous hormone in the range 0.01-1 nM. Half-maximal inhibition of binding was observed with 0.12 nM salmon calcitonin. Scatchard analysis of the data suggested the presence of one class of binding sites with a mean affinity constant of 0.9 X 10(10) M-1 and a mean receptor number of 40 X 10(8)/mg of protein. The binding of salmon calcitonin was highly specific; half-maximal inhibition of binding was observed with 63.8 nM bovine calcitonin, the hormone corticotropin having no effect in this system.
在从正常猪肺获得的亚细胞组分中研究了鲑鱼降钙素的结合情况。只有膜组分（密度为1.14 g/cm³）显示出对降钙素的特异性结合。125I标记的鲑鱼降钙素的特异性结合受到浓度范围为0.01 - 1 nM的未标记同源激素的竞争性抑制。用0.12 nM鲑鱼降钙素观察到结合抑制的半数最大值。对数据的Scatchard分析表明存在一类结合位点，其平均亲和常数为0.9×10¹⁰ M⁻¹，平均受体数为40×10⁸/毫克蛋白质。鲑鱼降钙素的结合具有高度特异性；用63.8 nM牛降钙素观察到结合抑制的半数最大值，促肾上腺皮质激素在该系统中没有作用。
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