Purification and characterization of glutathione reductase from rainbow trout (Oncorhynchus mykiss) liver and inhibition effects of metal ions on enzyme activity
Glutathione reductase (EC: 1.8. 1.7; GR) was purified from rainbow trout (Oncorhynchus
mykiss) liver, and some characteristics of the enzyme were investigated. The purification
procedure consisted of four steps: preparation of homogenate, ammonium sulfate
fractionation, affinity chromatography on 2′, 5′-ADP Sepharose-4B and gel filtration
chromatography on Sephadex G-200. The enzyme, with a specific activity of 27.45 U/mg
protein, was purified 1,654-fold with a yield of 41%. Optimal pH, stable pH, optimal …
mykiss) liver, and some characteristics of the enzyme were investigated. The purification
procedure consisted of four steps: preparation of homogenate, ammonium sulfate
fractionation, affinity chromatography on 2′, 5′-ADP Sepharose-4B and gel filtration
chromatography on Sephadex G-200. The enzyme, with a specific activity of 27.45 U/mg
protein, was purified 1,654-fold with a yield of 41%. Optimal pH, stable pH, optimal …
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