Among different proteins of blood, albumin is consider ased a unique protein due to having special properties. It is synthesized in the liver hepatocytes and is responsible for over 80% of plasma colloid osmotic pressure. It is used for critical disease. There are various ways to produce albumin in the world, each of which has its own oubenefitstand and defects. Meanwhile, a common method- which is often used for the production of albumin is a combination of Cohn and types of chromatography for the production of albumin is often used. In this study, to concexamisne the production of plasma products, especially albumin, we employed one conventional method with by creating changes.
Materials and Methods: In this research, the albumin was purified from human serum using chilled ethanol, accompanyinged withby chromatographic methods. We applied SDS-PAGE for a purity evaluation of the chromatographic process.
Results: SDS-PAGE showed that the purity of purified human albumin was about 99% . Purified human albumin by ion exchange chromatography showed a single bond with a molecular weight of 66 KDa. WB analysis confirmed the production of albumin.
Conclusion: Some of the advantages of this method includes: quick separation, safety of therapeutic product, ethanffordabil is cheapty and readily availability of ethanol, suitabileity for major laboratory approach, structurally simpleicity, high sensitivity and efficiency, cost-effectiveness and economicaly, and causthe of high purity and yield its can be an alternative ftor other methods. In one speechummary, this method can be a robust technique for protein plasma purification.