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Volumn 20, Issue 4, 1996, Pages 616-620

Use of a 96-well format for the affinity purification of maltose-binding protein (MBP) fusion proteins

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; COMPLEMENTARY DNA; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; RECOMBINANT PROTEIN;

EID: 0029964397     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (10)
  • 1
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    • Amann, E.1    Brosius, J.2
  • 2
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    • Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12
    • Duplay, P., H. Bedouelle, A. Fowler, I. Zabin, W. Saurin and M. Hofnung. 1984. Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12. J. Biol Chem. 259.10606-10613.
    • (1984) 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
  • 3
    • 0027170349 scopus 로고
    • Echinococcus multilocularis: Molecular and immunochemical characterization of diagnostic antigen II/3-10
    • Felleisen, R. and B. Gottstein. 1993. Echinococcus multilocularis: molecular and immunochemical characterization of diagnostic antigen II/3-10. Parasitology 107:335-342.
    • (1993) Parasitology , vol.107 , pp. 335-342
    • Felleisen, R.1    Gottstein, B.2
  • 4
    • 0029147898 scopus 로고
    • Protective immune mechanisms against Echinocuccus multilocularis
    • Gottstein, B. and R. Felleisen. 1995. Protective immune mechanisms against Echinocuccus multilocularis. Parasitol. Today 11:320-326.
    • (1995) Parasitol. Today , vol.11 , pp. 320-326
    • Gottstein, B.1    Felleisen, R.2
  • 5
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • Guan, C., P. Li, P.D. Riggs and H. Inouye. 1987. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67:21-30.
    • (1987) Gene , vol.67 , pp. 21-30
    • Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 6
    • 0020347668 scopus 로고
    • Maltose binding protein from E. coli
    • Kellerman, O.K. and T. Ferenci. 1982. Maltose binding protein from E. coli. Methods Enzymol. 90:459-463.
    • (1982) Methods Enzymol. , vol.90 , pp. 459-463
    • Kellerman, O.K.1    Ferenci, T.2
  • 7
    • 0024215242 scopus 로고
    • A vector to express and purify foreign proteins in Escherichia coli by fusion to, and separation from, maltose binding protein
    • Maina, C.V., P.D. Riggs, A.G. Grandea III, B.E. Slatko, L.S. Moran, J.A. Tagliamonte, L.A. McReynolds and C. Guan. 1988. A vector to express and purify foreign proteins in Escherichia coli by fusion to, and separation from, maltose binding protein. Gene 74:365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea III, A.G.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    Guan, C.8
  • 8
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    • Bacterial expression systems as tools for the production of immunodiagnostic parasite antigens
    • Müller, N. and R. Felleisen. 1995. Bacterial expression systems as tools for the production of immunodiagnostic parasite antigens. Parasitol. Today 11:476-480.
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    • Müller, N.1    Felleisen, R.2
  • 9
    • 0021153567 scopus 로고
    • Generation of β-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli
    • Nagai, K. and H.C. Thøgersen. 1984. Generation of β-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli. Nature 309:810-812.
    • (1984) Nature , vol.309 , pp. 810-812
    • Nagai, K.1    Thøgersen, H.C.2
  • 10
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    • Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli
    • Nagai, K. and H.C. Thøgersen. 1987. Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli. Methods Enzyraol. 153:461-481.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.