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

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 585 amino-acid chain, weighing 66.5 kD. Albumin molecule also has 17 di-sulfide bridges which form a stable spherical protein structure, which it cause of 80% of oncotic blood pressure. The aim of this study was to separate albumin from the human plasma by using ethanol at low temperature. Fresh frozen plasma was used as the starting material. In this study, albumin was separated from human plasma by using ethanol (commercial grade with 94-96% 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. Albumin was prepared with 5 and 20 percent concentrations. Quality comparison of the two concentrations showed a purity of more than 95%. The average yields of the 5 % and 20 % albumin preparations were 71% and 75.5%, respectively. Our data show that the produced albumin has a purity of higher than 95% and contains less than 5% polymer. In preparation of 5 % 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 4.7, instead of 6.5, in order to avoid bacterial contamination.