메뉴 건너뛰기




Volumn 134, Issue 1, 1998, Pages 103-114

Evaluation of genetically attached histidine affinity tails for purification of lactate dehydrogenase from transgenic tobacco

Author keywords

Immobilized metal affinity chromatography; Lactate dehydrogenase; Metal affinity precipitation; Polyhistidine tails; Tobacco

Indexed keywords

COBALT; HISTIDINE; LACTATE DEHYDROGENASE; NICKEL; POLYPEPTIDE; TOBACCO; ZINC;

EID: 0344625399     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(98)00050-8     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 0030029354 scopus 로고    scopus 로고
    • Enhanced NaCl stress tolerance in transgenic tobacco expressing bacterial choline dehydrogenase
    • Lilius G., Holmberg N., Bülow L. Enhanced NaCl stress tolerance in transgenic tobacco expressing bacterial choline dehydrogenase. Bio/Technology. 14:1996;177-180.
    • (1996) Bio/Technology , vol.14 , pp. 177-180
    • Lilius, G.1    Holmberg, N.2    Bülow, L.3
  • 2
    • 0030890431 scopus 로고    scopus 로고
    • Transgenic tobacco expressing Vitreoscilla hemoglobin exhibits enhanced growth and altered secondary metabolite production
    • Holmberg N., Lilius G., Bailey J., Bülow L. Transgenic tobacco expressing Vitreoscilla hemoglobin exhibits enhanced growth and altered secondary metabolite production. Nature Biotechnol. 15:1997;244-247.
    • (1997) Nature Biotechnol. , vol.15 , pp. 244-247
    • Holmberg, N.1    Lilius, G.2    Bailey, J.3    Bülow, L.4
  • 5
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt A., Cafferkey R., Bowdish K. Production of antibodies in transgenic plants. Nature. 342:1989;76-78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Cafferkey, R.2    Bowdish, K.3
  • 6
    • 0026071781 scopus 로고
    • Metal-affinity separations: A new dimension in protein processing
    • Arnold F.H. Metal-affinity separations: A new dimension in protein processing. Bio/Technology. 9:1991;151-156.
    • (1991) Bio/Technology , vol.9 , pp. 151-156
    • Arnold, F.H.1
  • 7
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath J., Carlsson J., Olsson I., Belfrage G. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature. 258:1975;598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 8
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E., Döbeli H., Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J. Chromatogr. 411:1987;177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Döbeli, H.2    Schacher, A.3
  • 9
    • 0025420050 scopus 로고
    • Engineering proteins for purification
    • Sassenfeld H.M. Engineering proteins for purification. Trends Biotechnol. 8:1990;88-93.
    • (1990) Trends Biotechnol. , vol.8 , pp. 88-93
    • Sassenfeld, H.M.1
  • 10
    • 0024296676 scopus 로고
    • Chelating peptide-immobilized metal ion affinity chromatography
    • Smith M.C., Furman T.C., Ingolia T.D., Pidgeon C. Chelating peptide-immobilized metal ion affinity chromatography. J. Biol. Chem. 263:1988;7211-7215.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7211-7215
    • Smith, M.C.1    Furman, T.C.2    Ingolia, T.D.3    Pidgeon, C.4
  • 11
  • 13
    • 0025925381 scopus 로고
    • 3-His sites in α-helices of synthetic metal-binding bovine somatotropin
    • 3-His sites in α-helices of synthetic metal-binding bovine somatotropin. Protein Eng. 4:1991;301-305.
    • (1991) Protein Eng. , vol.4 , pp. 301-305
    • Suh, S.-S.1    Haymore, B.L.2    Arnold, F.H.3
  • 14
    • 0030220473 scopus 로고    scopus 로고
    • A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand
    • Schmidt A.M., Müller H.N., Skerra A. A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand. Chem. Biol. 3:1996;645-653.
    • (1996) Chem. Biol. , vol.3 , pp. 645-653
    • Schmidt, A.M.1    Müller, H.N.2    Skerra, A.3
  • 15
    • 0025782267 scopus 로고
    • Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails
    • Lilius G., Persson M., Bülow L., Mosbach K. Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails. Eur. J. Biochem. 198:1991;499-504.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 499-504
    • Lilius, G.1    Persson, M.2    Bülow, L.3    Mosbach, K.4
  • 16
    • 15844412754 scopus 로고    scopus 로고
    • Affinity precipitation and site-specific immobilization of proteins carrying polyhistidine tails
    • Carlsson J., Mosbach K., Bülow L. Affinity precipitation and site-specific immobilization of proteins carrying polyhistidine tails. Biotech. Bioeng. 51:1996;221-228.
    • (1996) Biotech. Bioeng. , vol.51 , pp. 221-228
    • Carlsson, J.1    Mosbach, K.2    Bülow, L.3
  • 17
    • 0022913008 scopus 로고
    • Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene
    • Barstow D.A., Clark A.R., Chia W.N., Wigley D., Sharman A.F., Holbrook J.J., Atkinson T., Minton N.P. Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene. Gene. 46:1986;47-55.
    • (1986) Gene , vol.46 , pp. 47-55
    • Barstow, D.A.1    Clark, A.R.2    Chia, W.N.3    Wigley, D.4    Sharman, A.F.5    Holbrook, J.J.6    Atkinson, T.7    Minton, N.P.8
  • 18
    • 0027332853 scopus 로고
    • Zinc ions bound to chimeric His4/lactate dehydrogenase facilitate decarboxylation of oxaloacetate
    • Carlsson H., Prachayasittikul V., Bülow L. Zinc ions bound to chimeric His4/lactate dehydrogenase facilitate decarboxylation of oxaloacetate. Protein Eng. 6:1993;907-911.
    • (1993) Protein Eng. , vol.6 , pp. 907-911
    • Carlsson, H.1    Prachayasittikul, V.2    Bülow, L.3
  • 20
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucoronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson R.A., Kavanagh T.A., Bevan M.W. GUS fusions: beta-glucoronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6:1987;3901-3907.
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 21
    • 0023850178 scopus 로고
    • Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase
    • Saiki R.K., Mullis K.B., Erlich H.A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science. 239:1988;487-491.
    • (1988) Science , vol.239 , pp. 487-491
    • Saiki, R.K.1    Mullis, K.B.2    Erlich, H.A.3
  • 22
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou P.Y., Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. 47:1978;45-147.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-147
    • Chou, P.Y.1    Fasman, G.D.2
  • 23
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassay with tobacco tissue cultures
    • Murashige T., Skoog F. A revised medium for rapid growth and bioassay with tobacco tissue cultures. Physiol. Plant. 15:1962;473-497.
    • (1962) Physiol. Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 24
    • 0025245620 scopus 로고
    • The use of gene vectors in plant molecular biology
    • Walden R., Koncz C., Schell J. The use of gene vectors in plant molecular biology. Methods Mol. Cell. Biol. 1:1990;175-194.
    • (1990) Methods Mol. Cell. Biol. , vol.1 , pp. 175-194
    • Walden, R.1    Koncz, C.2    Schell, J.3
  • 25
    • 0025978277 scopus 로고
    • A simple and rapid method for the preparation of plant genomic DNA for PCR analysis
    • Edwards K., Johnstone C., Thompson C. A simple and rapid method for the preparation of plant genomic DNA for PCR analysis. Nucleic Acids Res. 19(6):1991;1349.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.6 , pp. 1349
    • Edwards, K.1    Johnstone, C.2    Thompson, C.3
  • 27
    • 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. 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.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0024306539 scopus 로고
    • Evaluation of the interaction of peptides with Cu(II), Ni(II) and Zn(II) by high-performance immobilized metal ion affinity chromatography
    • Yip T.-T., Nakagawa Y., Porath J. Evaluation of the interaction of peptides with Cu(II), Ni(II) and Zn(II) by high-performance immobilized metal ion affinity chromatography. Anal. Biochem. 183:1989;159-171.
    • (1989) Anal. Biochem. , vol.183 , pp. 159-171
    • Yip, T.-T.1    Nakagawa, Y.2    Porath, J.3
  • 30
    • 0023781763 scopus 로고
    • Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent
    • Hochuli E., Bannwarth W., Döbeli H., Gentz R., Stüber D. Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent. Bio/Technology. 6:1988;1321-1324.
    • (1988) Bio/Technology , vol.6 , pp. 1321-1324
    • Hochuli, E.1    Bannwarth, W.2    Döbeli, H.3    Gentz, R.4    Stüber, D.5
  • 31
    • 0021967194 scopus 로고
    • Purification of proteins by IMAC
    • Sulkowski E. Purification of proteins by IMAC. Trends Biotechnol. 3:1985;1-7.
    • (1985) Trends Biotechnol. , vol.3 , pp. 1-7
    • Sulkowski, E.1
  • 32
    • 0025789750 scopus 로고
    • The oligopeptide gly-pro-gly-pro-ala-gly-pro-gly-pro increases the internal proline level and improves osmotolerance when expressed in E. coli
    • Bülow L., Mosbach K. The oligopeptide gly-pro-gly-pro-ala-gly-pro-gly-pro increases the internal proline level and improves osmotolerance when expressed in E. coli. Gene. 109:1991;125-129.
    • (1991) Gene , vol.109 , pp. 125-129
    • Bülow, L.1    Mosbach, K.2
  • 33
    • 14744283294 scopus 로고
    • Protein stabilization by engineered metal chelation
    • Kellis J.T., Jr R.J. Todd, F.H. Arnold, Protein stabilization by engineered metal chelation. Bio/Technology. 9:1991;994-995.
    • (1991) Bio/Technology , vol.9 , pp. 994-995
    • Kellis, J.T.1    Todd R.J., Jr.2    Arnold, F.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.