title: Use of thiopropyl sepharose for the synthesis of an adsorbent for the affinity chromatography of glutathione S-transferase.
abstract: Thiopropyl Sepharose 6B in the 2-thiopyridyl-activated form was used for the reversible immobilisation of reduced glutathione (GSH). The resulting affinity matrix was successfully tested as a sorbent for the partial purification of glutathione S-transferase (GST) from pig kidney. The specific elution of the enzyme was performed with 10 mM GSH in Tris-HCl buffer (pH 7.8), non-specific elution with 20 mM dithiotreitol (DTT) in the same buffer.
authors.affiliation: Department of Biochemistry, Masaryk University, Brno, Czech Republic.
authors.forename: Z
authors.initials: Z
authors.lastname: Glatz
authors.forename: J
authors.initials: J
authors.lastname: Psotová
authors.forename: O
authors.initials: O
authors.lastname: Janiczek
authors.forename: K
authors.initials: K
authors.lastname: Chroust
authors.forename: T
authors.initials: T
authors.lastname: Jowet
mesh_terms: D000818:Animals; D002021:Buffers; D002846:Chromatography, Affinity / Q000379:methods; D005978:Glutathione / Q000737:chemistry; D005982:Glutathione Transferase / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology; D012685:Sepharose / Q000031:analogs & derivatives* / Q000737:chemistry; D013552:Swine
chemical_list: D002021:Buffers; C035872:thiopropyl-sepharose; D012685:Sepharose; D005982:Glutathione Transferase; D005978:Glutathione