Figures & data
Table I. The molecular weight distribution of poly-hemoglobin and final products based on optimal process (n = 3).
Figure 5. Secondary structure of final products with circular dichroism (A). Compared with the secondary structure of the storma-free human placenta hemoglobin (B), the secondary structure of final products is consistent. This can be very obviously explained by the process of crosslinking without disrupting the secondary structure.
![Figure 5. Secondary structure of final products with circular dichroism (A). Compared with the secondary structure of the storma-free human placenta hemoglobin (B), the secondary structure of final products is consistent. This can be very obviously explained by the process of crosslinking without disrupting the secondary structure.](/cms/asset/10168125-1f0f-4345-a261-88350f8b87bb/ianb_a_11116910_f0005_b.gif)