title: Purification of kappa-opioid receptor subtype to apparent homogeneity from frog brain.
abstract: Kappa-opioid receptor subtype was purified from digitonin solubilized preparation of frog brain membranes by hydrophobic and Sepharose 6B chromatography. 4800-fold purification over the membrane-bound receptors was achieved. The kappa receptor activity resides in a homo-oligomer of a single polypeptide of Mr 65,000.
authors.affiliation: Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged.
authors.forename: A
authors.initials: A
authors.lastname: Borsodi
authors.forename: A
authors.initials: A
authors.lastname: Khan
authors.forename: J
authors.initials: J
authors.lastname: Simon
authors.forename: S
authors.initials: S
authors.lastname: Benyhe
authors.forename: J
authors.initials: J
authors.lastname: Hepp
authors.forename: M
authors.initials: M
authors.lastname: Wollemann
authors.forename: K
authors.initials: K
authors.lastname: Medzihradszky
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D011893:Rana esculenta; D011957:Receptors, Opioid / Q000302:isolation & purification* / Q000378:metabolism; D017473:Receptors, Opioid, kappa
chemical_list: D011957:Receptors, Opioid; D017473:Receptors, Opioid, kappa