2000年6月23日
Stimuli-responsive separation of proteins using immobilized liposome chromatography
Journal of Chromatography B: Biomedical Sciences and Applications
- ,
- ,
- ,
- 巻
- 743
- 号
- 1-2
- 開始ページ
- 85
- 終了ページ
- 91
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/S0378-4347(00)00061-X
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. © 2000 Elsevier Science B.V.
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. © 2000 Elsevier Science B.V.
- リンク情報
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- DOI
- https://doi.org/10.1016/S0378-4347(00)00061-X
- CiNii Articles
- http://ci.nii.ac.jp/naid/80011815620
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/10942275
- URL
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0034705701&origin=inward
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=0034705701&origin=inward
- ID情報
-
- DOI : 10.1016/S0378-4347(00)00061-X
- ISSN : 1387-2273
- CiNii Articles ID : 80011815620
- PubMed ID : 10942275
- SCOPUS ID : 0034705701