Evidence for glutathione-S-transferase activity in human blood platelets.

Data will be presented pointing to the presence of glutathione-S-transferase activity in human blood platelets and the possible involvement of this enzyme in the process of platelet activation. Using 1-chloro-2,4-dinitrobenzene as a synthetic substrate of the glutathione-S-transferase a rapid dose-dependent depletion of platelet glutathione was measured. The formed GSH-CDNB conjugate was separated by thin-layer chromatography. Hints to the formation of leukotriene-like substances by glutathione-S-transferase catalysed reaction were obtained using the specific leukotriene C antagonist FPL 55 712 in aggregation studies.