Study Of Glutaraldehyde-polymerized Porcine Hemoglobin As Hemoglobin-based Oxygen Carrier

Transfusion therapy was one of important way on clinic. But nearly twenty years, the risk of transmission of infection in transfused blood brought much trouble on transfusion. Therefore, to search a sort of blood substitutes which were safety and abundant was the purpose of leechdom research and exploiture, especially Hemoglobin-based Oxygen Carrier (HBOCs).Using pig blood as the raw material, ultra-pure porcine hemoglobin was obtained through multiple purification steps;with glutaraldehyde as the cross-linker, polymerized porcine hemoglobin (pPolyHb) was then produced. Various physical and chemical properties, such as purity of the purified pHb, molecular weight distribution of pPolyHb, oxygen affinity and auto-oxidation tendency of the proteins were analyzed. Various properties of human, porcine and bovine red blood cell were analyzed.Pure porcine hemoglobin in solution was termer, and purity was attained to 99.9%. Glutaraldehyde-polymerized porcine hemoglobin was composed of hemoglobin polymers of various molecular sizes. There was no visible difference in the UV-visible absorption pattern between pHb and pPolyHb. At low temperatures, such as 4 °C, pHb was relatively stable against auto-oxidation. However, the polymerization increased the tendency of auto-oxidation of the products.Cell membrane phospholipids of human and porcine were similar, and the same as red blood cell proteins of human and porcine. Human and porcine hemoglobin were regulated by 2,3-DPG Bovine hemoglobin was regulated by C1-. Compared to porcine hemoglobin, oxygen affinity of pPolyHb was increased, and Hill coefficient was decreased.Porcine hemoglobin has high oxygen affinity, similar to that of humanhemoglobin and much higher than that of bovine hemoglobin. Polymerization with glutaraldehyde as the cross-linker increases the oxygen affinity and reduces the coefficient of the polymerized hemoglobin products. Rich supply, the unique properties of oxygen affinity and relative stability of porcine hemoglobin could make this type of protein a useful material in molecular design and large-scale production of HBOCs.