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A high-capacity hydrophobic adsorbent for human serum albumin

Authors
Journal
Analytical Biochemistry
0003-2697
Publisher
Elsevier
Publication Date
Volume
151
Issue
2
Identifiers
DOI: 10.1016/0003-2697(85)90201-5
Keywords
  • Hydrophobic Chromatography
  • Protein Processing
  • Albumin
  • Ceruloplasmin
  • α-1 Antitrypsin
  • Cohn Fractions Iv And V
Disciplines
  • Biology

Abstract

Abstract A simple method, based on salting out hydrophobic interaction chromatography, for the efficient removal of trace amounts of serum albumin from partially purified protein preparations is described. The method is also successfully applied for the purification of albumin from Cohn fraction IV, a by-product obtained from the commercial fractionation of human serum proteins by the ethanol precipitation procedure. About 70% of the adsorbed albumin can be eluted by buffer of low ionic strength and can thus be lyophilized directly, if required. The adsorbent can be used for several cycles of adsorption and desorption without affecting its selectivity or capacity. Its adsorption properties and capacity for serum albumin are compared with those of the commercially available adsorbent Blue Sepharose CL-6B.

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