Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography.

摘要: A scheme is described for the large scale purification of thioredoxin, thioredoxin reductase, and glutathione reductase. The based on an initial separation from two reductases by affinity chromatography agarose-bound N6-(6-aminohexyl)-adenosine 2',5'-bisphosphate (agarose-2',5'-ADP). were then separated hydrophobic purified separately to homogeneity. Thioredoxin was homogeneity immunoadsorption agarose containing immobilized goat anti-thioredoxin. Overall yields reductase exceeded 80% in each case. Both exhibit absorption band at approximately 320 nm which appears due a residual amount tightly bound NADP. Presence this has no apparent effect specific activity either enzyme.