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Effects of Some Metal Ions on Human Erythrocyte Glutathione Reductase:An In Vitro Study

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In this study, we investigated inhibitory effects of some metal ions on human erythrocyte glutathione reductase. For this purpose, initially human erythrocyte glutathione reductase was purified 1051-fold in a yield of 41% by using 2', 5'-ADP Sepharose 4B affinity gel and Sephadex G-200 gel filtration chromatography. SDS polyacrylamide gel electrophoresis was done in order to control the purification of enzyme. SDS polyacrylamide gel electrophoresis showed a single band for enzyme. A constant temperature (4°C) was maintained during the purification process. Enzyme activity was determined with the Beutler method by using a spectrophotometer at 340 nm. Hg2+, Cd2+, Pb2+, Cu2+, Fe3+ and Al3+ exhibited inhibitory effects on the enzyme in vitro.

Ki constants and IC50 values for metal ions were determined by Lineweaver-Burk graphs and plotting activity % vs. [I]. IC50 values of Pb2+, Hg2+, Cu2+, Cd2+ , Fe3+ and Al3+ were 0.011, 0.020, 0.0252, 0.0373, 0.209 and 0.229 mM, and the Ki constants 0.0254±0.0027, 0.0378±0.0043, 0.0409±0.0048, 0.0558±0.0083, 0.403±0.043 and 1.137±0.2 mM, respectively. While Pb2+, Hg2+, Cd2+ and Fe3+ showed competitive inhibition, others displayed noncompetitive inhibition.

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Keywords: Glutathione reductase; Human; Inhibition; metal ions

Document Type: Research Article

Publication date: 2007-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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