Immobilized liposome chromatography for refolding and purification of protein

Makoto Yoshimoto, Toshinori Shimanouchi, Hiroshi Umakoshi, Ryoichi Kuboi

研究成果査読

34 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)93-99
ページ数7
ジャーナルJournal of Chromatography B: Biomedical Sciences and Applications
743
1-2
DOI
出版ステータスPublished - 6月 23 2000
外部発表はい

ASJC Scopus subject areas

  • 化学 (全般)

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