title: Reconstitution of the 9 S estrogen receptor with heat shock protein 90.
abstract: As a first step in the investigation of the reconstitution of steroid hormone receptor systems, we studied the reconstitution of 9 S estrogen receptor (ER) from purified vero ER, which is the estradiol binding subunit, and heat shock protein 90 (hsp 90). By using a phosphate buffer containing molybdate, thiocyanate, dimethylformamide, glycerol, etc., vero ER could be converted to 9 S ER with hsp 90, but not with the control protein, ovalbumin. Inactivation of ER during the reconstitution was suppressed partially by hsp 90, but not by ovalbumin. Like native 8 S ER, the reconstituted ER was sedimented at about 8.9 S and 4.6 S on glycerol gradient centrifugation in low and high salt buffers, respectively.
authors.affiliation: Department of Biochemistry, Faculty of Science, Niigata University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Inano
authors.forename: M
authors.initials: M
authors.lastname: Haino
authors.forename: M
authors.initials: M
authors.lastname: Iwasaki
authors.forename: N
authors.initials: N
authors.lastname: Ono
authors.forename: T
authors.initials: T
authors.lastname: Horigome
authors.forename: H
authors.initials: H
authors.lastname: Sugano
mesh_terms: D000818:Animals; D002417:Cattle; D002499:Centrifugation, Density Gradient; D005260:Female; D006360:Heat-Shock Proteins / Q000502:physiology*; D011960:Receptors, Estrogen / Q000378:metabolism*
chemical_list: D006360:Heat-Shock Proteins; D011960:Receptors, Estrogen