Journal
SCIENCE OF THE TOTAL ENVIRONMENT
Volume 248, Issue 1, Pages 45-50Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0048-9697(99)00548-3
Keywords
lead effect; glutathione; reductase; peroxidase; transferase; whole blood
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Incubation of human whole blood for 24 h at 37 degrees C in the presence of 100-400 mu g/dl lead chloride or lead acetate caused a concentration-dependent decrease in the level of reduced glutathione up to 40%. Similarly, the activities of glutathione reductase,,glutathione peroxidase and glutathione S-transferase were decreased up to 25%, 50%, and 19%, respectively. Moreover, 100 mu g/dl lead chloride or lead acetate slowed the process of glutathione regeneration, and delayed the time for complete regeneration from 20 to 40 min. When glutathione S-transferase was purified by affinity chromatography on Sepharose-linked glutathione, incubated with lead chloride or lead acetate, a concentration-dependent inhibition of the enzymatic activity was observed reaching 50% inhibition at a lead salt concentration of 6000 mu g/dl. (C) 2000 Elsevier Science B.V. All rights reserved.
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