Abstract: Glutathione S-transferase was purified from human
erythrocytes and effects of some polyphenols were investigated on
the enzyme activity. The purification procedure was performed on
Glutathione-Agarose affinity chromatography after preparation of
erythrocytes hemolysate with a yield of 81%. The purified enzyme
showed a single band on the SDS-PAGE. The effects of some
poliphenolic compounds such as catechin, dopa, dopamine, progallol
and catechol were examined on the in vitro GST activity. Catechin
was determined to be inhibitor for the enzyme, but others were not
effective on the enzyme as inhibitors or activators. IC50 value -the
concentration of inhibitor which reduces enzyme activity by 50%-
was estimated to be 10 mM. Ki constants were also calculated as 6.38
± 0,70 mM with GSH substrate, and 3.86 ± 0,78 mM with CDNB
substrate using the equations of graphs for the inhibitor, and its
inhibition type was determined as non-competitive.