Christina Lind

TL;DR: The results support the earlier proposal that DT-diaphorase serves as a cellular control device against quinone toxicity and reflects the relative contributions of the two pathways.

TL;DR: The ability to chemically tag, select, and identify S-glutathionylated proteins, particularly during constitutive metabolism, will greatly enhance efforts to establish posttranslational redox modification of cellular proteins as an important biochemical control mechanism in coordinating cellular function.

TL;DR: The introduction of affinity chromatography for the purification of DTdiaphorase reduced the number of purification steps considerably and the key isolation step is the biospecific adsorption of the enzyme to immobilized dicoumarol, which is a potent competitive inhibitor of the enzymes with respect to NAD(P)H.

TL;DR: The combination of DT diaphorase and SOD is an efficient system for maintaining cDAoQ in its fully reduced state, a prerequisite for detoxication of the quinone by conjugation with sulfate or glucuronic acid.

TL;DR: The data indicate the complexity of mechanisms likely to be involved in regulating cellular proteins during oxidative stress and implicate controlled enzyme-catalysed S-glutathionylation as a potential selectivity factor in the redox modification of protein function by glutathione.