Selective Recovery of Proteins by Control of Their Surface Properties Utilizing PEG-Bound Affinity Ligands.
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- Kuboi Ryoichi
- Department of Chemical Science and Engineering, Osaka University
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- Hasegawa Tetsuhiro
- Department of Chemical Science and Engineering, Osaka University
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- Yamahara Katsuhito
- Department of Chemical Science and Engineering, Osaka University
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- Komasawa Isao
- Department of Chemical Science and Engineering, Osaka University
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- Johansson Göte
- Department of Biochemistry, University of Lund
書誌事項
- タイトル別名
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- Selective Recovery of Proteins by Contr
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Selective recovery of proteins by control of their surface properties is investigated by using a ligand modified aqueous two-phase system (ATPS) and polyethylene glycol (PEG) precipitation. The ligands used were nonionic surfactant (Triton and PEG-palmitate) and PEG-bound dye (Cibacron Blue and Procion Yellow). Both the partition coefficient in ATPS and the solubility in a PEG solution of Bovine Serum Albumin (BSA) increase significantly with the addition of these ligands, because the surface net hydrophobicity of BSA is increased by the binding of these hydrophobic ligands. On the other hand, these ligands have no effect on the partition behavior and solubility of Carbonic Anhydrase (CAB) and Ovalbumin (OvA), which have no binding sites to the ligands. Control of the surface properties of protein by these specific bindings of ligands can be utilized to improve the separation efficiency in ATPS and PEG precipitation. A separation process using ligand modified ATPS and PEG precipitation is developed.
収録刊行物
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- JOURNAL OF CHEMICAL ENGINEERING OF JAPAN
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JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 31 (4), 618-625, 1998
公益社団法人 化学工学会
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詳細情報 詳細情報について
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- CRID
- 1390001204565615872
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- NII論文ID
- 10002066057
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- NII書誌ID
- AA00709658
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- COI
- 1:CAS:528:DyaK1cXls1Kjsbk%3D
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- ISSN
- 18811299
- 00219592
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- NDL書誌ID
- 4541607
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- 抄録ライセンスフラグ
- 使用不可