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Glutathione conjugates. Immobilized enzyme synthesis and characterization by fast atom bombardment mass spectrometry

Pallante, S.L.; Lisek, C.A.; Dulik, D.M.; Fenselau, C.

Drug Metabolism and Disposition the Biological Fate of Chemicals 14(3): 313-318

1986

ISSN/ISBN: 0090-9556
PMID: 2872031
Document Number: 268065
Glutathione transferase activity was shown to be present in an immobilized preparation of microsomal protein. Chlorodinitrobenzene, ethacrynic acid, captopril, styrene oxide, and iminocyclophosphamide were found to be substrates, each providing a different kind of electrophilic functional group for conjugation. The glutathione conjugates were characterized by thin layer chromatography (visualized by reaction with ninhydrin) and by high pressure liquid chromatography. A variety of conditions was evaluated for analysis of these glutathiones by fast atom bombardment mass spectrometry.

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