Purification of recombinant protein A by aqueous two‐phase extraction integrated with affinity precipitation

Masamichi Kamihira, Rajni Kaul, Bo Mattiasson

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

Aqueous two‐phase extraction incorporated affinity precipitation was examined as a technique for protein purification. An enteric coating polymer, Eudragit S100, was employed as a ligand carrier. Eudragit was specifically partitioned to the top phase in the aqueous two‐phase systems. For application of this method to purification of recombinant protein A using human IgG coupled to Eudragit in an aqueous two‐phase system, 80% of protein A added was recovered with 81% purity. The purity was enhanced 26‐fold by thid method. The IgG‐Eudragit could be used repeatedly for the purification process. This seperation method should be applicable to industrial‐scale purification as a new purification procedure combining the advantages and compensating for the disadvantages of the aqueous two‐phase method and affinity precipitation method. © 1992 John Wiley & Sons, Inc.

Original languageEnglish
Pages (from-to)1381-1387
Number of pages7
JournalBiotechnology and Bioengineering
Volume40
Issue number11
DOIs
Publication statusPublished - Jan 1 1992
Externally publishedYes

Fingerprint

Recombinant proteins
Staphylococcal Protein A
Recombinant Proteins
Purification
Proteins
Polymers
Immunoglobulin G
Ligands
Coatings
methylmethacrylate-methacrylic acid copolymer

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

Purification of recombinant protein A by aqueous two‐phase extraction integrated with affinity precipitation. / Kamihira, Masamichi; Kaul, Rajni; Mattiasson, Bo.

In: Biotechnology and Bioengineering, Vol. 40, No. 11, 01.01.1992, p. 1381-1387.

Research output: Contribution to journalArticle

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