✦ LIBER ✦

Purification and characterization of glutathione reductase from calf liver. An improved procedure for affinity chromatography on 2′,5′-ADP-Sepharose 4B

✍ Scribed by Inger Carlberg; Bengt Mannervik

Publisher: Elsevier Science
Year: 1981
Tongue: English
Weight: 454 KB
Volume: 116
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(81)90398-5

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✦ Synopsis

Glutathione reductase has been purified to at least 98% homogeneity from calf liver. An essential part in the procedure involves affinity chromatography on 2',5'-ADP-Sepharose 4B to which the enzyme remains bound in the presence of 0.4 M phosphate. This step separates glutathione reductase from the closely related thioredoxin reductase. Some of the physical and catalytic properties as well as the amino acid composition of the enzyme are reported.