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Properties and physiological function of a glutathione reductase purified from spinach leaves by affinity chromatography

Planta

Jan 1, 1978

Barry Halliwell, Christine Helen Foyer

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Abstract

Glutathione reductase (EC 1.6.4.2) was purified from spinach (Spinacia oleracea L.) leaves by affinity chromatography on ADP-Sepharose. The purified enzyme has a specific activity of 246 enzyme units/mg protein and is homogeneous by the criterion of polyacrylamide gel electrophoresis on...read more

Mentioned in this Paper

Hydrogen Peroxide
Enzymes, antithrombotic
Glutathione Reductase
Enzymes, peripheral vasodilators
Glyceraldehyde-3-phosphate dehydrogenase
Fructose
Glutathione Disulfide
Dithiothreitol
NADP
NADH
Paper Details
References
  • References22
  • Citations71
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Properties and physiological function of a glutathione reductase purified from spinach leaves by affinity chromatography

Planta

Jan 1, 1978

Barry Halliwell, Christine Helen Foyer

PMID: 24414099

DOI: 10.1007/bf00390803

Abstract

Glutathione reductase (EC 1.6.4.2) was purified from spinach (Spinacia oleracea L.) leaves by affinity chromatography on ADP-Sepharose. The purified enzyme has a specific activity of 246 enzyme units/mg protein and is homogeneous by the criterion of polyacrylamide gel electrophoresis on...read more

Mentioned in this Paper

Hydrogen Peroxide
Enzymes, antithrombotic
Glutathione Reductase
Enzymes, peripheral vasodilators
Glyceraldehyde-3-phosphate dehydrogenase

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Paper Details
References
  • References22
  • Citations71
12345...

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