Use of thiopropyl sepharose for the synthesis of an adsorbent for the affinity chromatography of glutathione S-transferase

J Chromatogr B Biomed Sci Appl. 1997 Jan 24;688(2):239-43. doi: 10.1016/s0378-4347(96)00267-8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Buffers
  • Chromatography, Affinity / methods
  • Glutathione / chemistry
  • Glutathione Transferase / isolation & purification*
  • Hydrogen-Ion Concentration
  • Kidney / enzymology
  • Sepharose / analogs & derivatives*
  • Sepharose / chemistry
  • Swine

Substances

  • Buffers
  • thiopropyl-sepharose
  • Sepharose
  • Glutathione Transferase
  • Glutathione