Immobilized liposome chromatography for refolding and purification of protein

Makoto Yoshimoto, Toshinori Shimanouchi, Hiroshi Umakoshi, Ryoichi Kuboi

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)


Small unilamellar liposomes were utilized as a kind of aqueous two-phase system and artificial chaperone which specifically recognize protein conformation with fluctuated structure. Liposomes showed highly selective binding ability to conformationally changed proteins treated with various concentrations of guanidinium hydrochloride, as evaluated by immobilized liposome chromatography (ILC). In refolding of proteins, liposomes bound to refolding intermediate of proteins and prevented them from forming intermolecular aggregates. Refolding of bovine carbonic anhydrase, lysozyme and ribonuclease A was significantly improved in the presence of liposomes. Furthermore, by utilizing ILC, refolding of proteins was also successfully and simply carried out with considerable high reactivation yield.

Original languageEnglish
Pages (from-to)93-99
Number of pages7
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Issue number1-2
Publication statusPublished - Jun 23 2000
Externally publishedYes


  • Immobilized liposome chromatography
  • Lipid bilayer membranes
  • Protein refolding

ASJC Scopus subject areas

  • General Chemistry


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