메뉴 건너뛰기




Volumn 10, Issue 3, 1997, Pages 309-319

High-level expression of soluble protein in Escherichia coli using a His6-Tag and maltose-binding-protein double-affinity fusion system

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

EID: 0031214792     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0759     Document Type: Article
Times cited : (216)

References (21)
  • 2
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides inEscherichia coli
    • di Guan C., Li P., Riggs P. D., Inouye H. Vectors that facilitate the expression and purification of foreign peptides inEscherichia coli. Gene. 67:1988;21-30.
    • (1988) Gene , vol.67 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 3
    • 0021252896 scopus 로고
    • Sequences of the malE gene and of its product, the maltose-binding protein ofEscherichia coli
    • Duplay P., Bedouelle H., Fowler A., Zabin I., Saurin W., Hofnung M. Sequences of the malE gene and of its product, the maltose-binding protein ofEscherichia coli. J. Biol. Chem. 259:1988;10606-10613.
    • (1988) J. Biol. Chem. , vol.259 , pp. 10606-10613
    • Duplay, P.1    Bedouelle, H.2    Fowler, A.3    Zabin, I.4    Saurin, W.5    Hofnung, M.6
  • 4
    • 0001895061 scopus 로고
    • Expression and purification of maltose-binding protein fusions
    • New York: Greene Assoc./Wiley Interscience
    • Riggs P. D. Expression and purification of maltose-binding protein fusions. Current Protocols in Molecular Biology. 1992;Greene Assoc./Wiley Interscience, New York.
    • (1992) Current Protocols in Molecular Biology
    • Riggs, P.D.1
  • 5
    • 0025754301 scopus 로고
    • The 2.3 Å resolution structure of the maltose- Or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino J. C., Lu G.-Y., Quiocho F. A. The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266:1991;5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 6
    • 0021062151 scopus 로고
    • Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
    • Miller D. M. III, Olson J. S., Pflugrath J. W., Quiocho F. A. Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258:1983;13665-13672.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13665-13672
    • Miller D.M. III1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 8
    • 0021361020 scopus 로고
    • Low-affinity penicillin-binding protein associated with β-lactam resistance inStaphylococcus aureus
    • Hartman B. J., Tomasz A. Low-affinity penicillin-binding protein associated with β-lactam resistance inStaphylococcus aureus. J. Bacteriol. 158:1984;513-516.
    • (1984) J. Bacteriol. , vol.158 , pp. 513-516
    • Hartman, B.J.1    Tomasz, A.2
  • 10
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed inEscherichia coliS
    • Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed inEscherichia coliS. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 11
    • 0029379678 scopus 로고
    • High-yield expression, refolding and purification of penicillin-binding protein 2a from methicillin-resistantStaphylococcus aureus
    • Frank L. J., Wisniewski D., Hammond G. G., Hermes J., Marcy A., Cameron P. M. High-yield expression, refolding and purification of penicillin-binding protein 2a from methicillin-resistantStaphylococcus aureus. Protein Expression Purif. 6:1995;671-678.
    • (1995) Protein Expression Purif. , vol.6 , pp. 671-678
    • Frank, L.J.1    Wisniewski, D.2    Hammond, G.G.3    Hermes, J.4    Marcy, A.5    Cameron, P.M.6
  • 12
    • 0026681666 scopus 로고
    • New vectors for high level expression of recombinant proteins in bacteria
    • Hakes D. J., Dixon J. E. New vectors for high level expression of recombinant proteins in bacteria. Anal. Biochem. 202:1992;293-298.
    • (1992) Anal. Biochem. , vol.202 , pp. 293-298
    • Hakes, D.J.1    Dixon, J.E.2
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0017584161 scopus 로고
    • Construction and characterization of new cloning vehicles. II. A multipurpose cloning system
    • Bolivar F., Rodriguez R. L., Greene P. J., Betlach M. C., Heyneker H. L., Boyer H. W. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene. 2:1977;95-113.
    • (1977) Gene , vol.2 , pp. 95-113
    • Bolivar, F.1    Rodriguez, R.L.2    Greene, P.J.3    Betlach, M.C.4    Heyneker, H.L.5    Boyer, H.W.6
  • 18
    • 0014202305 scopus 로고
    • Characterization byin vitroEscherichia coli
    • Ullmann A., Jacob F., Monod J. Characterization byin vitroEscherichia coli. J. Mol. Biol. 24:1967;339-342.
    • (1967) J. Mol. Biol. , vol.24 , pp. 339-342
    • Ullmann, A.1    Jacob, F.2    Monod, J.3
  • 19
    • 0029077340 scopus 로고
    • Over-production, purification, and properties of the uridine-diphosphate-NLEscherichia coli
    • Liger D., Masson A., Blanot D., Van Heijenoort J., Parquet C. Over-production, purification, and properties of the uridine-diphosphate-NLEscherichia coli. Eur. J. Biochem. 230:1995;80-87.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 80-87
    • Liger, D.1    Masson, A.2    Blanot, D.3    Van Heijenoort, J.4    Parquet, C.5
  • 20
    • 0030066560 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of UDP-NLEscherichia coli
    • Gubler M., Appoldt Y., Keck W. Overexpression, purification, and characterization of UDP-NLEscherichia coli. J. Bacteriol. 178:1996;906-910.
    • (1996) J. Bacteriol. , vol.178 , pp. 906-910
    • Gubler, M.1    Appoldt, Y.2    Keck, W.3
  • 21
    • 0030020538 scopus 로고    scopus 로고
    • Biochemical evidence for the formation of a covalent acyl phosphate linkage between UDP-NL
    • Falk P. J., Ervin K. M., Volk K. S., Ho H.-T. Biochemical evidence for the formation of a covalent acyl phosphate linkage between UDP-NL. Biochemistry. 35:1996;1417-1422.
    • (1996) Biochemistry , vol.35 , pp. 1417-1422
    • Falk, P.J.1    Ervin, K.M.2    Volk, K.S.3    Ho, H.-T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.