Purification Process for Heat Shock Proteins Using Aqueous Two-Phase System and PEG Fractional Precipitation.
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- Kuboi Ryoichi
- Department of Chemical Engineering, Osaka University
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- Hasegawa Tetsuhiro
- Department of Chemical Engineering, Osaka University
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- Yano Koji
- Department of Chemical Engineering, Osaka University
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- Komasawa Isao
- Department of Chemical Engineering, Osaka University
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A simple and effective purification process for heat shock proteins (HSPs), in which PEG fractional precipitation was combined with an aqueous two-phase system (ATPS), was successfully developed based upon the proteins’ molecular surface properties. Both GroEL and GroES, typical HSPs from E. coli, were selectively partitioned to the PEG (top) phase of the ATPS. GroEL and GroES were selectively and stepwisely concentrated from the above PEG phase by PEG fractional precipitation. In addition, the purification of GroEL and GroES as a complex by using biospecific affinity with adenosine triphosphate (ATP) was achieved. GroEL and GroES can be purified either as individual native molecules or as a 1:1 complexed state by the control of ATP addition.
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 28 (6), 797-802, 1995
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
- 1390282679543724416
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- NII論文ID
- 10002135025
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- NII書誌ID
- AA00709658
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- COI
- 1:CAS:528:DyaK28XhvFajsA%3D%3D
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- ISSN
- 18811299
- 00219592
- http://id.crossref.org/issn/00219592
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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
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可