Molecular characterization of a corticotropin (ACTH) receptor.
We have used a new methodology to generate a monospecific antiserum to the corticotropin (ACTH) receptor on mouse Y-1 adrenal cells. Using immunoaffinity chromatography the ACTH receptor was purified, and the molecular structure and 125I-ACTH binding characteristics were determined. A molecular weight (Mr) of 225 000 was determined for the complete ACTH receptor as analyzed by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The receptor was composed of 4 subunits with Mr 83 000, 64 000, 52 000 and 22 000. The 83 and 52 kDa subunits were disulfide linked and non-covalently associated with the 64 and 22 kDa subunits. The ability to specifically bind 125I-ACTH was localized to the 83 kDa subunit. The purified receptor possessed binding affinities of 3.4 X 10(10) M-1 and 1.0 X 10(9) M-1 as determined by Scatchard analysis.
D000310:Adrenal Gland Neoplasms; D000818:Animals; D002478:Cells, Cultured; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007120:Immunochemistry; D051379:Mice; D008970:Molecular Weight; D011956:Receptors, Cell Surface / Q000032:analysis* / Q000378:metabolism; D018043:Receptors, Corticotropin
D011956:Receptors, Cell Surface; D018043:Receptors, Corticotropin