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. 2013 Aug 26;8(8):e72075. doi: 10.1371/journal.pone.0072075

Figure 4. ANS Fluorescence studies.

Figure 4

(a) Relative ANS fluorescence of Hb as a function of glyoxal before [⧫] and after centrifugation [◊]. Error bars represent the mean ± SD (n = 3). *Significance p<0.05 with respect to control (b) ANS fluorescence emission spectra of native Hb in absence of glyoxal (curve 1); in the presence of 20% glyoxal (curves 2) and 70% glyoxal (curve 3). The excitation wavelength was 380 nm and emission wavelength was in the range 400–600 nm. The protein concentration was 3 µM and the path length was 1 cm. (c) Relative ANS fluorescence of Hb as a function of increasing days at 30% [♦] and 40% [▪] glyoxal excited at 280 nm at 37°C. The protein concentration was 8 µM and the path length was 1 cm. Error bars represent the mean ± SD (n = 3). *Significance p<0.05 with respect to control.