| Literature DB >> 462920 |
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 is described. It consists of two purification steps, namely, precipitation of most of the other plasma proteins from a 3-fold diluted plasma with ethanol at 42% concentration, pH 5.75 and -5 degrees C, leaving over 96% pure albumin in the supernatant, followed by isoelectric precipitation of albumin from the supernatant at pH 4.8 and -5 degrees 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 are also discussed.Entities:
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Year: 1979 PMID: 462920 DOI: 10.1111/j.1423-0410.1979.tb04441.x
Source DB: PubMed Journal: Vox Sang ISSN: 0042-9007 Impact factor: 2.144