Abstract
Glutathione has been covalently bound to cellulose via the linking reagent s-triazine trichloride (sTT) in three ways: the tripeptide through its sulfur and either reduced or oxidized glutathione through its amino nitrogen. The use of glutathione-bound cellulose in chromatography was studied with bovine serum albumin (BSA) and glutathione reductase. The enzyme was eluted with 1 M NaCl.
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Danner, J., Lenhoff, H.M. & Heagy, W. Glutathione-bound celluloses: Preparation with the linking reagent S-triazine trichloride and use in chromatography. Journal of Solid-Phase Biochemistry 1, 177–188 (1976). https://doi.org/10.1007/BF02991015
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DOI: https://doi.org/10.1007/BF02991015