RT Journal Article
SR Electronic
T1 Glutathione conjugates. Immobilized enzyme synthesis and characterization by fast atom bombardment mass spectrometry.
JF Drug Metabolism and Disposition
JO Drug Metab Dispos
FD American Society for Pharmacology and Experimental Therapeutics
SP 313
OP 318
VO 14
IS 3
A1 S L Pallante
A1 C A Lisek
A1 D M Dulik
A1 C Fenselau
YR 1986
UL http://dmd.aspetjournals.org/content/14/3/313.abstract
AB 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.