Interaction of acrylamide with glutathione in rat erythrocytes |
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Authors: | Rakesh Dixit Mukul Das Prahlad K. Seth Hasan Mukhtar |
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Affiliation: | Industrial Toxicology Research Centre, P.O. Box No. 80, Mahatma Gandhi Marg, Lucknow 226001 India |
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Abstract: | Evidence is presented for an enzyme-catalyzed conjugation of acrylamide (ACR) in rat erythrocytes. Daily exposure of rats to ACR for a period of 7, 14 and 21 days resulted in a time-dependent decrease in glutathione content. In vitro incubation of ACR with rat erythrocytes suspension caused a concentration-dependent decrease in glutathione levels. Red blood cell (RBC) enzyme-catalyzed conjugation of ACR with glutathione increased with protein concentration and was dependent on pH and time of incubation. Glutathione-S-transferase (GST) activity using acrylamide and 1-chloro 2,4-dinitrobenzene (CDNB) as substrates followed the order: liver > kidney > brain > erythrocytes. Glutathione peroxidase activity of RBCs was inhibited by the in vitro addition of ACR to erythrocytes. These results suggest that rat erythrocytes are equipped with the mechanism which can inactivate toxic electrophilic chemicals, such as acrylamide. |
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Keywords: | Reduced glutathione glutathione reductase red blood cells ACR acrylamide CDNB 1-chloro 2,4-dinitrobenzene DTNB 5,5′-dithio-2-nitro-benzoic acid GSH reduced glutathione GST RBC red blood cells TCA trichloroacetic acid |
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