title: Variation in the molecular mass of the Ah receptor among vertebrate species and strains of rats.
abstract: 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.
mesh_terms: D000818:Animals; D002642:Chick Embryo; D006224:Cricetinae; D003600:Cytosol / Q000378:metabolism; D005796:Genes; D005799:Genes, Dominant; D006168:Guinea Pigs; D006838:Hydrocarbons / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008647:Mesocricetus; D051379:Mice; D008810:Mice, Inbred C57BL; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains; D018336:Receptors, Aryl Hydrocarbon; D011955:Receptors, Drug / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D013045:Species Specificity
chemical_list: D006838:Hydrocarbons; D018336:Receptors, Aryl Hydrocarbon; D011955:Receptors, Drug