PT  - JOURNAL ARTICLE
AU  - S L Pallante
AU  - C A Lisek
AU  - D M Dulik
AU  - C Fenselau
TI  - Glutathione conjugates. Immobilized enzyme synthesis and characterization by fast atom bombardment mass spectrometry.
DP  - 1986 May 01
TA  - Drug Metabolism and Disposition
PG  - 313--318
VI  - 14
IP  - 3
4099  - http://dmd.aspetjournals.org/content/14/3/313.short
4100  - http://dmd.aspetjournals.org/content/14/3/313.full
SO  - Drug Metab Dispos1986 May 01; 14
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.