Poland A, Glover E
Biochem Biophys Res Commun. 1987 Aug 14;146(3):1439-49. doi: 10.1016/0006-291x(87)90811-4.
The Ah receptor in eight vertebrate species was characterized by labeling the cytosolic fraction of tissue with the photoaffinity ligand, [125I]-2-azido-3-iodo-7,8-dibromodibenzo-p-dioxin, and analysis of the products by denaturing gel electrophoresis. The apparent molecular mass of the dominant labeled peptide showed appreciable species variation: mouse-95 kDa; chicken (embryo)-101 kDa; guinea pig-103 kDa; rabbit-104 kDa; rat-106 kDa; human-106 kDa; monkey-113 kDa, and hamster-124 kDa. Seven inbred strains of rats, had a Ah receptor ligand binding peptide of 106 kDa; however outbred Long-Evans rats were shown to be polymorphic expressing a 101 kDa and/or 106 kDa allelic forms. The notable frequency of structural variation in the Ah receptor is in contrast to the analogous highly conserved steroid hormone receptors.
通过用光亲和配体[125I]-2-叠氮基-3-碘-7,8-二溴二苯并-对-二恶英标记组织的胞质部分，并通过变性凝胶电泳分析产物，对八个脊椎动物物种中的芳烃受体进行了表征。主要标记肽的表观分子量显示出明显的物种差异：小鼠为95 kDa；鸡（胚胎）为101 kDa；豚鼠为103 kDa；兔为104 kDa；大鼠为106 kDa；人类为106 kDa；猴为113 kDa，仓鼠为124 kDa。七个近交系大鼠具有106 kDa的芳烃受体配体结合肽；然而，远交系Long-Evans大鼠表现出多态性，表达101 kDa和/或106 kDa的等位基因形式。芳烃受体结构变异的显著频率与类似的高度保守的甾体激素受体形成对比。
