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Wiadomosci lekarskie (Warsaw, Poland : 1960)

Here we determined the rate constants for the individual redox reactions between the two redox-sensitive cysteinyl residues of roGFP2 and the active-site cysteinyl residues of the model class I glutaredoxin PfGrx from the malaria parasite Plasmodium falciparum using stopped-flow kinetic measurements in combination with redox mobility shift assays

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1 2 Convex Analysis in General Vector Spaces

Regarding intracellular roGFP2-based structure-function analysis of glutaredoxins, we now showed that the GSSG-dependent oxidation of the fused glutaredoxin moiety (and not the glutathionylation of the roGFP2 moiety) is rate-limiting unless saturating GSSG concentrations are present