A high-yield one-step purification method using copper-chelating chromatography for recombinant proteins fused with maltose-binding protein

Analytical Biochemistry

Volumn 358, Issue 1, 2006, Pages 152-154

  Lee, Ka Ming ^a   Ma, Kit Wan ^a   Shaw, Pang Chui ^a   Wong, Kam Bo ^a  

^a CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER;

HIGH YIELD; MALTOSE BINDING PROTEINS; ONE-STEP PURIFICATION;

RECOMBINANT PROTEINS;

BACTERIAL PROTEIN; BACTERIUM LYSATE; CARRIER PROTEIN; COPPER; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; RECOMBINANT PROTEIN; RIBOSOME PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CHROMATOGRAPHY; COPPER CHELATING CHROMATOGRAPHY; PRIORITY JOURNAL; PROTEIN PURIFICATION;

EID: 33749445807     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.08.007     Document Type: Article

References (12)

1. di Guan C., Li P., Riggs P.D., and Inouye H. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67 (1988) 21-30
2. Maina C.V., Riggs P.D., Grandea III A.G., Slatko B.E., Moran L.S., Tagliamonte J.A., McReynolds L.A., and Guan C.D. An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene 74 (1988) 365-373
3. Riggs P. Expression and purification of maltose-binding protein fusions. Current Protocols. Molecular Biology vol. 16.6 (1994), Greene Associates/Wiley Interscience, New York 1-14
4. Routzahn K.M., and Waugh D.S. Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins. J. Struct. Funct. Genom. 2 (2002) 83-92
5. Ashraf S.S., Benson R.E., Payne E.S., Halbleib C.M., and Gron H. A novel multi-affinity tag system to produce high levels of soluble and biotinylated proteins in Escherichia coli. Protein Expr. Purif. 33 (2004) 238-245
6. Sachdev D., and Chirgwin J.M. Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin. Protein Expr. Purif. 12 (1998) 122-132
7. Kapust R.B., and Waugh D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8 (1999) 1668-1674
8. Pryor K.D., and Leiting B. High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding protein double-affinity fusion system. Protein Expr. Purif. 10 (1997) 309-319
9. Raha M., Kawagishi I., Muller V., Kihara M., and Macnab R.M. Escherichia coli produces a cytoplasmic α-amylase, AmyA. J. Bacteriol. 174 (1992) 6644-6652
10. Tchorzewski M., Boldyreff B., Issinger O., and Grankowski N. Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: Evaluation by the two hybrid system. Int. J. Biochem. Cell. Biol. 32 (2000) 737-746
11. Gonzalo P., Lavergne J.P., and Reboud J.P. Pivotal role of the P1 N-terminal domain in the assembly of the mammalian ribosomal stalk and in the proteosynthetic activity. J. Biol. Chem. 276 (2001) 19762-19769
12. Shimizu T., Nakagaki M., Nishi Y., Kobayashi Y., Hachimori A., and Uchiumi T. Interaction among silkworm ribosomal proteins P1, P2 and P0 required for functional protein binding to the GTPase-associated domain of 28S rRNA. Nucleic Acids Res. 30 (2002) 2620-2627