메뉴 건너뛰기




Volumn 176, Issue 1-2, 1996, Pages 249-255

A multifunctional vector system for heterologous expression of proteins in Escherichia coli. Expression of native and hexahistidyl fusion proteins, rapid purification of the fusion proteins, and removal of fusion peptide by Kex2 protease

Author keywords

Affinity purification; Co expression vector; Expression in Escherichia coli; Hexahistidyl fusion protein; Hit 1 protein; Kex2 protease; Multifunctional expression vector; PLC( 1); Sequence specific proteolysis

Indexed keywords

HYBRID PROTEIN; NICKEL; PHOSPHOLIPASE C; PROTEINASE; ZINC;

EID: 0030591758     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1119(96)00260-0     Document Type: Article
Times cited : (42)

References (20)
  • 1
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0026532760 scopus 로고
    • Structural and enzymatic characterization of a purified prohormone-processing enzyme: Secreted, soluble Kex2 protease
    • Brenner, C. and Fuller, R.S. (1992) Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease. Proc. Natl. Acad. Science USA 89, 922-926.
    • (1992) Proc. Natl. Acad. Science USA , vol.89 , pp. 922-926
    • Brenner, C.1    Fuller, R.S.2
  • 3
    • 0025976716 scopus 로고
    • Effects of second-codon mutations on expression of the insulin-like growth factor-II-encoding gene in Escherichia coli
    • Cantrell, A.S., Burgett, S.G., Cook, J.A., Smith, M.C. and Hsiung, H.M. (1991) Effects of second-codon mutations on expression of the insulin-like growth factor-II-encoding gene in Escherichia coli. Gene 98, 217-223.
    • (1991) Gene , vol.98 , pp. 217-223
    • Cantrell, A.S.1    Burgett, S.G.2    Cook, J.A.3    Smith, M.C.4    Hsiung, H.M.5
  • 4
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in E. coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan, K.L. and Dixon, J.E. (1991) Eukaryotic proteins expressed in E. coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192, 262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 5
    • 0023615233 scopus 로고
    • Expression of bovine growth hormone derivatives in Escherichia coli and the use of derivatives to produce natural sequence growth hormone by cathepsm C cleavage
    • Hsiung, H.M. and MacKellar, W.C. (1987) Expression of bovine growth hormone derivatives in Escherichia coli and the use of derivatives to produce natural sequence growth hormone by cathepsm C cleavage. Meth. Enzymol. 153, 390-401.
    • (1987) Meth. Enzymol. , vol.153 , pp. 390-401
    • Hsiung, H.M.1    MacKellar, W.C.2
  • 6
    • 0026651651 scopus 로고
    • Ty element induced temperature-sensitive mutations of Saccharomyces cerevisiae
    • Kawakami, K., Shafer, B.K., Garfinkel, D.J., Strathern, J.N. and Nakamura, Y. (1992) Ty element induced temperature-sensitive mutations of Saccharomyces cerevisiae. Genetics 131, 821-832.
    • (1992) Genetics , vol.131 , pp. 821-832
    • Kawakami, K.1    Shafer, B.K.2    Garfinkel, D.J.3    Strathern, J.N.4    Nakamura, Y.5
  • 8
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D. and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Meth. Enzymol. 154, 367-382.
    • (1987) Meth. Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 10
    • 0025782267 scopus 로고
    • Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails
    • Lilius, G., Person, M., Bülow, L. and Mosbach, K. (1991) Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails. Eur. J. Biochem. 198, 499-504.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 499-504
    • Lilius, G.1    Person, M.2    Bülow, L.3    Mosbach, K.4
  • 11
    • 0024841821 scopus 로고
    • Immobilization and affinity purification of recombinant proteins using histidinc peptide fusion
    • Ljungquist, C., Breitholtz, A., Brink-Nilsson, H., Moks, T., Uhlén, M. and Nilsson, B. (1989) Immobilization and affinity purification of recombinant proteins using histidinc peptide fusion. Eur. J. Biochem. 186, 563-569.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 563-569
    • Ljungquist, C.1    Breitholtz, A.2    Brink-Nilsson, H.3    Moks, T.4    Uhlén, M.5    Nilsson, B.6
  • 12
    • 0022390906 scopus 로고
    • A general method for saturation mutagenesis of cloned DNA fragments
    • Myers, R.M., Lerman, S.L. and Maniatis. T. (1985) A general method for saturation mutagenesis of cloned DNA fragments. Science 229,242-247.
    • (1985) Science , vol.229 , pp. 242-247
    • Myers, R.M.1    Lerman, S.L.2    Maniatis, T.3
  • 13
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • Parks, T.D., Leuther, K.K., Howard, E.D., Johnston, S.A. and Dougherty, W.G. (1994) Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal. Biochem. 216, 413-417.
    • (1994) Anal. Biochem. , vol.216 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 14
    • 0026970340 scopus 로고
    • Regulation of phospholipase Cδ activity by sphingomyelin and sphingosine
    • Pawelczyk, T. and Lowenstein, J.M. (1992) Regulation of phospholipase Cδ activity by sphingomyelin and sphingosine. Arch. Biochem. Biophys. 297, 328-333.
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 328-333
    • Pawelczyk, T.1    Lowenstein, J.M.2
  • 15
    • 0025923860 scopus 로고
    • γ1 isoform with tyrosine kinase
    • γ1 isoform with tyrosine kinase. TIBS 16, 297-301.
    • (1991) TIBS , vol.16 , pp. 297-301
    • Rhee, S.G.1
  • 18
    • 0024296676 scopus 로고
    • Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins
    • Smith, M.C., Thomas, F.C., Thomas, I.D. and Pidgeon, C. (1988) Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins. J. Biol. Chem. 263, 7211-7215.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7211-7215
    • Smith, M.C.1    Thomas, F.C.2    Thomas, I.D.3    Pidgeon, C.4
  • 20
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp18 and pUC19 vectors
    • Yannish-Perron, C., Viera, J. and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yannish-Perron, C.1    Viera, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.