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Original Articles

Processing of ferulic acid modified hemoglobin

, , , , &
Pages 1075-1079 | Received 02 Nov 2015, Accepted 28 Dec 2015, Published online: 02 Feb 2016

Figures & data

Figure 1. Synthesis of BAEGF.

Figure 1. Synthesis of BAEGF.

Figure 2. Synthesis of BAEGF-Hb.

Figure 2. Synthesis of BAEGF-Hb.

Figure 3. The IFE of Hb and BAEGF-Hb.

Figure 3. The IFE of Hb and BAEGF-Hb.

Figure 4. The standard curve of BAEGF.

Figure 4. The standard curve of BAEGF.

Figure 5. UV–vis wavelength scanning of BAEGF-Hb (line a) and Hb (line b).

Figure 5. UV–vis wavelength scanning of BAEGF-Hb (line a) and Hb (line b).

Figure 6. Oxygen binding curve of native Hb was measured using a Hemox analyzer at 37 °C in PBS, pH 7.4. Vertical axis is the fraction of hemoglobin sites to which oxygen is bound. The partial oxygen pressure at 50% saturation is expressed in mmHg.

Figure 6. Oxygen binding curve of native Hb was measured using a Hemox analyzer at 37 °C in PBS, pH 7.4. Vertical axis is the fraction of hemoglobin sites to which oxygen is bound. The partial oxygen pressure at 50% saturation is expressed in mmHg.

Figure 7. Oxygen binding curve of BAEGF-Hb was measured using a Hemox analyzer at 37 °C in PBS, pH 7.4.

Figure 7. Oxygen binding curve of BAEGF-Hb was measured using a Hemox analyzer at 37 °C in PBS, pH 7.4.

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