Separation of Albumin from the Human Plasma by Ethanol and Low Temperature

Background and Objective: Human plasma is a suitable source for different proteins and enzymes with a variety of therapeutic effects. Examples include coagulation factors VIII and IX, immunoglobulin, and albumin, which consists of a ۵۸۵ amino-acid chain, weighing ۶۶.۵ kD. Albumin molecule also has ۱۷ di-sulfide bridges which form a stable spherical protein structure, which it cause of ۸۰% of oncotic blood pressure. The aim of this study was to separate albumin from the human plasma by using ethanol at low temperature. Materials and Methods: Fresh frozen plasma was used as the starting material. In this study, albumin was separated from human plasma by using ethanol (commercial grade with ۹۴-۹۶% purity) in low temperature. By adjustment of different parameters such as pH, temperature, and concentration of alcohol, different factions of plasma can be separated which are from fraction I to fraction V. Fraction I is a good source for fibrinogen and coagulation factor VIII preparation, fraction II is suitable for preparation of immunoglobulin, and fraction V is a good source for albumin preparation. Results: Albumin was prepared with ۵ and ۲۰ percent concentrations. Quality comparison of the two concentrations showed a purity of more than ۹۵%. The average yields of the ۵ % and ۲۰ % albumin preparations were ۷۱% and ۷۵.۵%, respectively. Conclusion: Our data show that the produced albumin has a purity of higher than ۹۵% and contains less than ۵% polymer. In preparation of ۵ % albumin, it is possible to use lower concentrations of sodium caprylate as stabilizer. It has also been shown in the formulation that the preparation process can be started at the acidic pH of ۴.۷, instead of ۶.۵, in order to avoid bacterial contamination.

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Keywords: Purification ، Human plasma ، Protein ، Albumin