Solubilization and isolation of the human placenta receptor for epidermal growth factor-urogastrone.

摘要: We describe the solubilization and purification of both photoaffinity-labeled unlabeled human placenta receptor for epidermal growth factor-urogastrone (EGF-URO). The photolabeled can be purified 300- to 500-fold from membrane extracts by combined immunoaffinity lectin-agarose affinity chromatography. This isolation approaches theoretical purity. Upon gel filtration wheat germ agglutinin-Sepharose chromatography, EGF-URO binding activity co-migrate, as measured a newly developed immobilization assay binding. Sequential ion exchange, Cibacron blue-Sepharose, agglutinin-Sepharose, chromatography yield 110-fold activity; this fraction contains protein constituents that exhibit electrophoretic mobilities parallel those constituents, have apparent molecular weights 180,000 160,000. weight range is consistent with Stokes radius 5.1 nm (Sephacryl S-200 filtration), although an 4.3 estimated on Sepharose-6B. unaffected 2-mercaptoethanol. work provides basis further detailed studies factor receptor.