Mutation of surface-exposed histidine residues of recombinant human granulocyte-colony stimulating factor (Cys17Ser) impacts on interaction with chelated metal ions and refolding in aqueous two-phase systems
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概要
- 論文の詳細を見る
- 2003-03-25
著者
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LUKSA Virginijus
Institute of Biotechnology
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Bumelis Vladas
Sicor Biotech Uab Centre Of Research And Development
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ZAVECKAS Mindaugas
Institute of Biotechnology
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CHMIELIAUSKAITE Valerija
SICOR Biotech UAB, Centre of Research and Development
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ZVIRBLIS Gintautas
Institute of Biotechnology
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CHMIELIAUSKAITE Valerija
Institute of Biotechnology
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BUMELIS Vladas
Biotechna UAB, Centre of Research and Development
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PESLIAKAS Henrikas
Biotechna UAB, Centre of Research and Development
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Chmieliauskaite Valerija
Sicor Biotech Uab Centre Of Research And Development
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Zvirblis Gintautas
Sicor Biotech Uab Centre Of Research And Development
関連論文
- Chelated mercury as a ligand in immobilized metal ion affinity chromatography of proteins
- Effect of surface histidine mutations and their number on the partitioning and refolding of recombinant human granulocyte-colony stimulating factor (Cys17Ser) in aqueous two-phase systems containing chelated metal ions
- Mutation of surface-exposed histidine residues of recombinant human granulocyte-colony stimulating factor (Cys17Ser) impacts on interaction with chelated metal ions and refolding in aqueous two-phase systems
- Comparative studies of recombinant human granulocyte-colony stimulating factor, its Ser-17 and (His)_6-tagged forms interaction with metal ions by means of immobilized metal ion affinity partitioning Effect of chelated nickel and mercuric ions on extracti