Preparation of functional recombinant protein from E. coli using a nondetergent sulfobetaine

BioTechniques

Volumn 29, Issue 6, 2000, Pages 1166-1167

  Chong, Y ^a   Chen, H ^a  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

BETAINE DERIVATIVE; CCAAT ENHANCER BINDING PROTEIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; RECOMBINANT PROTEIN; SULFOBETAINE; UNCLASSIFIED DRUG;

ARTICLE; ESCHERICHIA COLI; NONHUMAN; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; SOLUBILIZATION;

ESCHERICHIA COLI;

EID: 0034532685     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/00296bm01     Document Type: Article

References (8)

1. Expression and characterization of the recombinant catalytic subunit of casein kinase 1I from the yeast Yarrowia lipolytica in Escherichia coli
2. Role of the transcription factor C/EBPβ in expression of a rat pregnancy-specific glycoprotein gene
3. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
4. The p50 subunit of NF-κB associates with the NF-IL6 transcription factor
5. Functional properties of the separate subunits of human DNA helicase II/Ku autoantigen
6. Non-detergent sulphobetaines: A new class of mild solubilization agents for protein purification
7. Halophilic protein stabilization by the mild solubilizing agents nondetergent sulfobetaines