Author/Authors :
-، - نويسنده Blood Transfusion Research Center, High Institute for Research and Education in Transfusion Medicine, Tehran, Iran Mousavi Hosseini, Kamran , -، - نويسنده Department of Biochemistry, Blood Transfusion Research Center, High Institute for Research and Education in Transfusion Medicine, P.O. Box 14665-1157, Tehran, I.R. IRAN Pourmokhtar, Mojgan , -، - نويسنده Department of Biotechnology, Blood Transfusion Research Center, High Institute for Research and Education in Transfusion Medicine, P.O. Box 14665-1157, Tehran, I.R. IRAN Habibi Roudkenar, Mehryar , -، - نويسنده Department of Biotechnology, Blood Transfusion Research Center, High Institute for Research and Education in Transfusion Medicine, P.O. Box 14665-1157, Tehran, I.R. IRAN Shahabi, Majid
Abstract :
Background: There are varieties of purification techniques for separation of human plasma proteins such as salting out, ion exchange chromatography, and ethanol fractionation. There are limitations for each method, for example in salting out method, the salt has to be removed in an additional step. Ion exchange chromatography is difficult for scaling up, and plasma fractionation is a time consuming method and it needs machinery and plant. In the present study the fractionation of human plasma by polyethylene glycol was investigated. Objectives: The purpose of this study was to investigate the possibility of the fractionation of human plasma by polyethylene glycol. Materials and Methods: Human plasma fractionation was carried out by using polyethylene glycol at different concentrations from five to twenty percent, and it was followed by centrifugation. After each step of addition of polyethylene glycol the supernatant was removed for further fractionation by addition of higher concentration of polyethylene glycol. Results: Suitable intermediate sources for protein purification were obtained by fractionation of human plasma by polyethylene glycol. Fibrinogen in fraction 5% , IgG and IgM in fraction 10%, IgA in fraction 20%, and finally albumin and α1-Antitrypsin in supernatant 20% of polyethylene glycol were achieved. Conclusion: By our study we could obtain four different fractions as intermediate sources for protein purification which cannot be easily obtained from plasma fractionation by cold ethanol fractionation.
