Glutathione reductase from germinated peas

3-Methyleneoxindole reductase of peas.

A 100-fold purification of a reduced triphosphopyridine nucleotide/3-methyleneoxindole reductase of peas has been achieved using conventional protein fractionation procedures. Reduced diphosphopyridine nucleotide is 25-fold less effective than reduced triphosphopyridine nucleotide as the reductant. The preparation is free of other reductase activities including those linking the oxidation of re...

A glutathione reductase from Escherichia coli.

Earlier studies had demonstrated that a flavoprotein capable of mediating a triphosphopyridine nucleotide (TPN)-linked reduction of Furacin (5-nitro-2-furaldehyde semicarbazone) was present in cell-free extracts of Furacin-susceptible strains of Escherichia coli, but was absent in extracts of resistant strains (I). Dr. Philip E. Hartman, who was then associated with our department, suggested to...

Mammalian Selenoprotein Thioredoxin-glutathione Reductase

Mitochondrial Thioredoxin-Glutathione Reductase from Larval Taenia crassiceps (Cysticerci)

Mitochondrial thioredoxin-glutathione reductase was purified from larval Taenia crassiceps (cysticerci). The preparation showed NADPH-dependent reductase activity with either thioredoxin or GSSG, and was able to perform thiol/disulfide exchange reactions. At 25 degrees C specific activities were 437 +/- 27 mU mg(-1) and 840 +/- 49 mU mg(-1) with thioredoxin and GSSG, respectively. Apparent K(m)...

Glutathione reductase from bakers' yeast and beef liver.

The reduction of glutathione by a heat-labile system in liver was discovered by Hopkins and Elliott (1). Later Mann (2) obtained a soluble enzyme preparation from liver which required, for the reduction process, a cofactor and glucose as hydrogen donor. Meldrum and Tarr (3) found that oxidized glutathione was reduced by rat blood and by yeast and demonstrated the function of TPNl as a cofactor ...