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Figure 2 | BMC Structural Biology

Figure 2

From: Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase

Figure 2

Effect of GSH on oligomeric status and enzymatic activity of Pf GST. A. Quenching of tryptophan fluorescenceintensity and enzymatic activity of tetrameric Pf GST withincreasing concentrations of GSH. In the figure, solid and hollow squares denote data for enzymatic activity and fluorescence, respectively. B. SEC profile of tetrameric Pf GST incubated with increasing concentrations of GSH for 2 h at 25°C and run in the same GSH containing buffer. In the figure, a-f represent curves for tetrameric Pf GST incubated with 0, 0.1, 0.2, 0.4, 0.6 and 2.0 mM GSH, respectively. The curves have been displaced on Y-axis for presentation. Inset shows the percent population of dimeric (solid squares) and tetrameric (hollow squares) species of Pf GST with increasing concentration of GSH based on the data obtained from the curves displayed in the main figure.

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