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Original Articles

Haemoglobin site-specifically modified with ferulic acid to suppress the autoxidation

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Pages 1077-1081 | Received 17 Feb 2017, Accepted 19 Mar 2017, Published online: 12 Apr 2017

Figures & data

Figure 1. Synthesis of BAEGF.

Figure 1. Synthesis of BAEGF.

Figure 2. Synthesis of FA-Hb.

Figure 2. Synthesis of FA-Hb.

Figure 3. Calibration working curve of BAEGF.

Figure 3. Calibration working curve of BAEGF.

Figure 4. UV-Vis wavelength scanning of Hb (line A) and FA-Hb (line B).

Figure 4. UV-Vis wavelength scanning of Hb (line A) and FA-Hb (line B).

Figure 5. Oxygen-binding curves of native Hb (a) and FA-Hb (b) were measured using a Hemox analyzer at 37 °C in PBS, pH 7.4. Vertical Axis is the fraction of haemoglobin sites to which oxygen is bound. The partial oxygen pressure at 50% saturation is expressed in mmHg.

Figure 5. Oxygen-binding curves of native Hb (a) and FA-Hb (b) were measured using a Hemox analyzer at 37 °C in PBS, pH 7.4. Vertical Axis is the fraction of haemoglobin sites to which oxygen is bound. The partial oxygen pressure at 50% saturation is expressed in mmHg.

Figure 6. Time course of MetHb formation in Hb and FA-Hb at 37 °C. (a) no NaN3; (b) with 0.1 mol/L NaN3.

Figure 6. Time course of MetHb formation in Hb and FA-Hb at 37 °C. (a) no NaN3; (b) with 0.1 mol/L NaN3.

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