Cover image of the article: Purification of Human Serum Albumin by Ion Exchange Chromatography

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Purification of Human Serum Albumin by Ion Exchange Chromatography

Authors

Nima Padashi1,*, Mehdi Arjmand2, Samira Rajaei3, Ali DabbaghAli Dabbagh ORCID4

Abstract

Introduction: Albumin, one of the most important plasma proteins, has a difficult process of synthesis and production. We compared two different methods for albumin purification: Carboxymethyl cellulose (CM cellulose) resin exchange and Diethylaminoethyl cellulose (DEAE cellulose) resin exchange in order to determine which resin could be more beneficial.Materials and methods: two ion exchange resins were used DEAE cellulose resin and CM cellulose resin. All resins were recruited according to the standard preparation protocol. The final results were analyzed using SDS-PAGE technique.Results: in DEAE Cellulose resin, nearly more than 75% of the purified protein was albumin; while, in CM cellulose resin, more than 90% was albumin.Conclusion: albumin purification using CM cellulose resin is much more efficacious compared to DEAE cellulose resin. Though significant laboratory findings were demonstrated in this study, clinical studies are needed to confirm clinical outcomes.?

Highlights

How to Cite:Padashi N, Arjmand M, Rajaei S, Dabbagh A. Purification of Human Serum Albumin by Ion Exchange Chromatography. J Cell Mol Anesth. 2016;1(4):e149524. doi: https://doi.org/10.22037/jcma.v1i4.13565

References

  • 1.
    References are in the PDF file of the article.

Copyright

© 2016, Author(s). This open-access article is available under the Creative Commons Attribution 4.0 (CC BY 4.0) International License (https://creativecommons.org/licenses/by/4.0/), which allows for unrestricted use, distribution, and reproduction in any medium, provided that the original work is properly cited.

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Nima PadashiPubMedScholar
Mehdi ArjmandPubMedScholar
Samira RajaeiPubMedScholar
Ali DabbaghPubMedScholar
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