Résumé
There are variety 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 plants. In the present study the fractionation of human plasma by polyethylene glycol was investigated. The purpose of this study was to investigate the possibility of the fractionation of human plasma by polyethylene glycol. Human plasma fractionation was carried out by using polyethylene glycol with different concentrations from five to twenty percent, followed by centrifugation. After centrifugation the supernatant was used for further fractionation by addition of a higher concentration of polyethylene glycol. 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 alpha1- Antitrypsin in supernatant 20% of polyethylene glycol were achieved. 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