Glutathione conjugates. Immobilized enzyme synthesis and characterization by fast atom bombardment mass spectrometry.
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.
Pallante
S L
SL
Lisek
C A
CA
Dulik
D M
DM
Fenselau
C
C
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
D004800:Enzymes, Immobilized; D005982:Glutathione Transferase; D005978:Glutathione