Abstract
A new method for the isolation of glutathione reductase which successively utilizes chromatography on 2'-5'-ADP-Sepharose 4B and DEAE-Sepharose CL 6B, is described. With these two steps, it was possible to purify to homogeneity the glutathione reductase from gerbil liver. Some molecular properties of the purified enzyme are reported.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Chromatography, Affinity / methods
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Chromatography, Ion Exchange / methods
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Ethanolamines
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Gerbillinae
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Glutathione Reductase / isolation & purification*
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Isoelectric Focusing
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Liver / enzymology*
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Sepharose / analogs & derivatives
Substances
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2',5'-ADP-sepharose
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Ethanolamines
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Sepharose CL 4B
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Sepharose
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Glutathione Reductase
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2-diethylaminoethanol