書誌事項
- タイトル別名
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- Purification of His–Tagged Protein Using an Immobilized NickelAffinity Porous Hollow–Fiber Membrane
- ニッケルイオン コテイ タコウセイ チュウクウシ マク オ モチイタ His tag タンパクシツ ノ アフィニティ セイセイ
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An immobilized metal affinity porous membrane of a hollow-fiber form was applied to the purification of geneticallyengineered histidine (His)–tagged fusion protein. An iminodiacetate (IDA)group (–N(CH2COOH)2)was introducedinto the poly–glycidyl methacrylate chain grafted onto a polyethylene-made porous hollow–fiber membrane.Subsequently, nickel ions were bound to the IDA group before the permeation of a His–tagged green fluorescent pro-tein (GFP)solution through the porous membrane. The resultant immobilized nickel affinity porous membrane(immobilized Ni membrane)had a ligand density of 0.36 mol/kg and a phosphate buffer flux of 0.4 m/h at a perme-ation pressure of 0.1 MPa and 298 K. His–tagged GFP adsorbed to the immobilized Ni membrane was eluted by per-meating a 0.5 M imidazole solution through the porous membrane. From an SDS–PAGE analysis, the purity of theprotein was found to be improved from 35 to 97%.
収録刊行物
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- 膜
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膜 34 (4), 233-238, 2009
日本膜学会
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詳細情報 詳細情報について
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- CRID
- 1390001206423840896
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- NII論文ID
- 10026336356
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- NII書誌ID
- AN0023215X
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- ISSN
- 18846440
- 03851036
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- NDL書誌ID
- 10385814
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可