Abstract
A simple method, based on ethanol fractionation, for the preparation of highly purified human serum albumin with a higher yield than that of the conventional ethanol procedures was described. It consists of 2 purification steps, i.e., precipitation of most of the other plasma proteins from a 3-fold diluted plasma with ethanol at 42% concentration, pH 5.75 and -5.degree. C, leaving over 96% pure albumin in the supernatant, at pH 4.8 and -5.degree. C. The paste thus obtained was processed to the final albumin solution according to the conventional methods. The yield of the final albumin with a purity of over 99% was equivalent to 29.5 g/l of plasma representing a recovery of over 93%. The possibility of recovering other plasma proteins and the suitability for large scale preparation were also discussed.