Stimuli-responsive separation of proteins using immobilized liposome chromatography

Toshinori Shimanouchi, Seiichi Morita, Hiroshi Umakoshi, Ryoichi Kuboi


22 被引用数 (Scopus)


The possibility of the stimuli-responsive separation of proteins was investigated using immobilized liposome chromatography (ILC) as novel aqueous two-phase systems. The specific capacity factor (k(s)) of β-galactosidase, obtained by analysis of ILC, was varied by changing the pH of the solution and was maximized at the specific pH of 5 (k(s, max) = 5.57). The k(s) values were found to correspond well with their local hydrophobicities, which can be determined by the aqueous two-phase partitioning method. The variation of k(s), therefore, indicates a change in the surface properties of a protein during conformational change under pH stimuli. A similar phenomenon is observed in the case of other proteins (α-glucosidase, k(s, max) = 11.3 at pH 4; carbonic anhydrase from bovine, k(s, max) = 6.53 at pH 4). The difference in the height and/or the position of the peaks of the k(s)-pH curves of each protein suggests a difference in their pH denaturation in the ILC column. Based on these results, the mutual separation of the above proteins at pH 4 could be successfully performed by selecting their specific capacity factor as a design parameter.

ジャーナルJournal of Chromatography B: Biomedical Sciences and Applications
出版ステータスPublished - 6月 23 2000

ASJC Scopus subject areas

  • 化学 (全般)


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