Figure 5
From: Structural basis of peroxidase catalytic cycle of human Prdx6
Determining Oligomeric Status of Prdx6 in Reduced and Oxidised State Using Electrophoretic, Spectroscopic and Chromatographic tools. (A) Native-PAGE (8%T/0.27%C) (top) and Protein/formaldehyde crosslinking followed by 12% SDS-PAGE (bottom) with reduced and oxidised Prdx6, (B) Hydrodynamic diameter (Hd) measurement by analysing size distribution by volume plot of reduced and oxidised Prdx6 using DLS, (C) Intact mass spectroscopic analysis of reduced Prdx6, and (D) Elution profile of Blue Dextran (monitored at 600 nm), reduced and oxidised Prdx6 (monitored at 280 nm) on sephadex G-75 column. {Note. R: Reduced Prdx6; O: Oxidised Prdx6; Rf: Reduced Prdx6 crosslinked with 0.6% formaldehyde; R′f: Reduced Prdx6 crosslinked with 1.2% formaldehyde; Of: Oxidised Prdx6 crosslinked with 0.6% formaldehyde; O′f: Oxidised Prdx6 crosslinked with 1.2% formaldehyde; CA, Carbonic Anhydrase (monomer: 25KDa); αLA, α-lactalbumin (monomer: 14KDa)}.
