Sheep brain glutathione reductase: Purification and general properties
- 19 June 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 250 (1) , 72-74
- https://doi.org/10.1016/0014-5793(89)80687-8
Abstract
Sheep brain glutathione reductase was purified about 11000-fold with an overall yield of 40%. The method included ammonium sulphate fractionation, heat denaturation, 2′,5′-ADP Sepharose 4B and Sephadex G-200 chromatography steps. Specific activity at the final step was 193 IU/mg. The M r of the enzyme was found to be 116000 by gel filtration chromatography. On SDS-PAGE, two identical subunits of M r 64000 were obtained. From the spectral data, about 2 mol FAD per mol of enzyme were calculated.Keywords
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