10 * 23000, SDS-PAGE, the wild type enzyme exists as a mixture of various forms, favoring the homodecamer at higher protein concentration and lower ionic salt concentration and in the presence of dithiothreitol
Prx IV oligomers contain two prevalent species with apparent molecular masses of 27 and 54 kDa corresponding to Prx IV monomers and disulfide-linked homodimers
2 * 24000, existed as a dimer under non-reducing conditions, and is dissociated into monomers by dithiothreitol. It might predominantly exist in oligomeric form, SDS-PAGE
2 * 22000, the homodimeric oxidized enzyme form is reduced to a monomeric form by thioredoxin and by dithiothreitol and is converted to a homodimeric oxidized form by H2O2, SDS-PAGE
composed of two identical octamers, 2-fold toroid-shaped structure with outer and inner diameters of 14 and 6 nm, respectively. Although oligomerization of individual subunits does not take place through an intersubunit-disulfide linkage involving Cys50 and Cys213, Cys50 is essential for the formation of the hexadecamer
composed of two identical octamers, 2-fold toroid-shaped structure with outer and inner diameters of 14 and 6 nm, respectively. Although oligomerization of individual subunits does not take place through an intersubunit-disulfide linkage involving Cys50 and Cys213, Cys50 is essential for the formation of the hexadecamer
glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation
the transition dimer-decamer produced in vitro between pH 7.5 and 8.0 suggests that a great change in the enzyme quarternary structure of the enzyme may take place in the chloroplast during the dark-light transition. The dimer-decamer equilibrium depends on NaCl concentration and concentration of dithiothreitol
recombinant cPrx I produces in Escherichia coli forms differently sized high molecular weight protein structures. cPrx I and cPrx II function both as peroxidases and as molecular chaperones. The peroxidase function predominates in the lower molecular weight forms, whereas the chaperone function predominates in the higher molecular weight complexes. Oxidative stress and heat shock exposure of yeasts cause the protein structures of cPrxl and cPrx II to shift from low MW species to high molecular weight complexes. This triggers a peroxidase-to-chaperone functional switch
reduced TpAhpC forms stable octamers or decamers in solution whereas oxidation generates a heterogeneous mixture of oligomeric species. TpAhpC undergoes redox-sensitive oligomer formation
reduced TpAhpC forms stable octamers or decamers in solution whereas oxidation generates a heterogeneous mixture of oligomeric species. TpAhpC undergoes redox-sensitive oligomer formation
primary structure and peptide mapping for detection of the disulfide-containing peptide, using chemical modification and tryptic digestion with HPLC-ESI-MS analyses, overview. Conformational analysis of XfPrxQ, modelling, overview
primary structure and peptide mapping for detection of the disulfide-containing peptide, using chemical modification and tryptic digestion with HPLC-ESI-MS analyses, overview. Conformational analysis of XfPrxQ, modelling, overview
1.11.1.24 thioredoxin-dependent peroxiredoxin
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