Abstract
Glutathione reductase from human leukocytes has been purified 570-fold by using the methods of ammonium sulfate fractionation (35–70%), CM-Sephadex column chromatography, and affinity chromatography. The molecular weight of the enzyme was determined by gel filtration on Sephadex G-200 and found to be 120,000 ⊣ 5000. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis the enzyme had a molecular weight of 19,000 ± 2000 when dissolved in 1% sodium dodecyl sulfate and 1% 2-mercaptoethanol. Velocity versus pH curve indicated that the enzyme may be a diprotic system.
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