title: Glutathione conjugates. Immobilized enzyme synthesis and characterization by fast atom bombardment mass spectrometry.
abstract: 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.
authors.forename: S L
authors.initials: SL
authors.lastname: Pallante
authors.forename: C A
authors.initials: CA
authors.lastname: Lisek
authors.forename: D M
authors.initials: DM
authors.lastname: Dulik
authors.forename: C
authors.initials: C
authors.lastname: Fenselau
mesh_terms: D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer / Q000379:methods; D004583:Electrons; D004800:Enzymes, Immobilized / Q000096:biosynthesis; D005069:Evaluation Studies as Topic; D005978:Glutathione / Q000302:isolation & purification / Q000378:metabolism*; D005982:Glutathione Transferase / Q000032:analysis / Q000378:metabolism / Q000502:physiology*; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure; D008297:Male; D013058:Mass Spectrometry / Q000379:methods; D008861:Microsomes / Q000201:enzymology; D011817:Rabbits; D013379:Substrate Specificity
chemical_list: D004800:Enzymes, Immobilized; D005982:Glutathione Transferase; D005978:Glutathione