Three-step chromatographic purification procedure for the porduction of a His-tag recombinant kinesin overexpressed in E. coli
スポンサーリンク
概要
- 論文の詳細を見る
- 2000-01-14
著者
-
Santarelli X.
Ecole Superieur De Technologie Des Biomolecules De Bordeaux(estbb) Universite Victor Segalen Bordeau
-
GIBERT S.
Laboratoire de Biologie Moleculaire et Immunolgie des Protozoaires Parasites, Universite Victor Sega
-
BAKALARA N.
Laboratoire de Biologie Moleculaire et Immunolgie des Protozoaires Parasites, Universite Victor Sega
-
Gibert S.
Laboratoire De Biologie Moleculaire Et Immunolgie Des Protozoaires Parasites Universite Victor Segal
-
Bakalara N
Univ. Victor Segalen Bordeaux 2 Bordeaux Fra
関連論文
- Efficient two-step chromatographic purification of penicillin acylase from clarified Escherichia coli ultrasonic homogenate
- Penicillin acylase purification with the aid of hydrophobic charge induction chromatography
- Cloning, expression and two-step purification of recombinant His-tag enhanced green fluorescent protein over-expressed in Escherichia coli
- Evaluation of immobilized metal affinity chromatography for purification of penicillin acylase
- Purification and on-column refolding of EGFP overexpressed as inclusion bodies in Escherichia coli with expanded bed anion exchange chromatography
- Evaluation of three expanded bed adsorption anion exchange matrices with the aid of recombinant enhanced green fluorescent protein overexpressed in Escherichia coli
- Three-step purification of bacterially expressed human single-chain Fv antibodies for clinical applications
- Three-step chromatographic purification procedure for the porduction of a His-tag recombinant kinesin overexpressed in E. coli
- Evaluation of chromatographic recycling for imidazole used in the chromatographic purification of His-tag recombinant proteins
- On-column refolding of an insoluble histidine tag recombinant exopolyphosphatase from Trypanosoma brucei overexpresed in Escherichia coli
- Characterization and application of new macroporous membrane ion exchangers