Abstract: The ability of agricultural and decorative plants to
absorb and detoxify TNT and RDX has been studied. All tested 8
plants, grown hydroponically, were able to absorb these explosives
from water solutions: Alfalfa > Soybean > Chickpea> Chikling vetch
>Ryegrass > Mung bean> China bean > Maize. Differently from
TNT, RDX did not exhibit negative influence on seed germination
and plant growth. Moreover, some plants, exposed to RDX
containing solution were increased in their biomass by 20%. Study of
the fate of absorbed [1-14ðí]-TNT revealed the label distribution in
low and high-molecular mass compounds, both in roots and above
ground parts of plants, prevailing in the later. Content of 14ðí in lowmolecular
compounds in plant roots are much higher than in above
ground parts. On the contrary, high-molecular compounds are more
intensively labeled in aboveground parts of soybean. Most part (up to
70%) of metabolites of TNT, formed either by enzymatic reduction
or oxidation, is found in high molecular insoluble conjugates.
Activation of enzymes, responsible for reduction, oxidation and
conjugation of TNT, such as nitroreductase, peroxidase,
phenoloxidase and glutathione S-transferase has been demonstrated.
Among these enzymes, only nitroreductase was shown to be induced
in alfalfa, exposed to RDX. The increase in malate dehydrogenase
activities in plants, exposed to both explosives, indicates
intensification of Tricarboxylic Acid Cycle, that generates reduced
equivalents of NAD(P)H, necessary for functioning of the
nitroreductase. The hypothetic scheme of TNT metabolism in plants
is proposed.
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.