Human albumin purification: a modified and concise method

ABSTRACT

Background: Among different proteins of blood, albumin is considered a unique protein due to having special properties. Now, various protocols are used for the albumin purification worldwide, each of them has its own advantages and disadvantages. Meanwhile, a common method which is often used for the production of albumin is a combination of Cohn along with different types of chromatography. The aim of the present study was to create a concise and cost-effective albumin purification method by employing a conventional method with some modifications.

Methods: In this research, the albumin was purified from human serum using chilled ethanol, followed by chromatographic methods. The purity of harvested albumin was evaluated by cellulose acetate membrane electrophoresis (CAME) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Western blotting (WB) analysis and thermostability were used for functional and stability measurement assessment, respectively.

Results: SDS-PAGE and CAME showed that the purity of purified human albumin was about 99%. Purified human albumin showed a single band with a molecular weight of 66 kDa. The results were validated by WB analysis .Also, the thermostability of purified albumin was same as the commercial albumin.

Conclusion: This method can be a robust technique for purification of albumin in order to use clinical and research approaches.

KEYWORDS:

• Albumin
• ethanol
• gel filtration
• ion exchange chromatography
• western blot
• purification

Acknowledgments

This study was supported by the Tabriz University of Medical Sciences and practical work was carried out in drug applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.

Conflict of interests

The authors have not declared any conflict of interest in this work.

Additional information

Funding

This work was supported by the Tabriz University of Medical Sciences.