title: Affinity purification of the mammalian beta-2-adrenergic receptor.
abstract: The efficiency of covalently linking alprenolol to Sepharose via a 14-atom spacer prepared from 1,4-butanediol diglycidyl ether has been increased. This in turn has aided in increasing the specific yield of beta-2-adrenergic receptor by a factor of 3 over earlier results. Further development of extraction and solubilization protocols are also described. The adsorption of the affinity-purified receptor to stainless steel was measured, and is cited as a potential problem in further purification by high-pressure liquid chromatography.
authors.affiliation: Department of Chemistry, University of Toronto, Mississauga, Canada.
authors.forename: J L
authors.initials: JL
authors.lastname: Tedesco
authors.forename: K M
authors.initials: KM
authors.lastname: Pearsall
authors.forename: M
authors.initials: M
authors.lastname: Thompson
authors.forename: U J
authors.initials: UJ
authors.lastname: Krull
mesh_terms: D000327:Adsorption; D000526:Alprenolol; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D007457:Iodine Radioisotopes; D008024:Ligands; D011943:Receptors, Adrenergic, beta / Q000302:isolation & purification*; D013193:Stainless Steel
chemical_list: D007457:Iodine Radioisotopes; D008024:Ligands; D011943:Receptors, Adrenergic, beta; D013193:Stainless Steel; D000526:Alprenolol