메뉴 건너뛰기




Volumn 51, Issue 2, 1996, Pages 221-228

Affinity precipitation and site-specific immobilization of proteins carrying polyhistidine tails

Author keywords

metal affinity precipitation; polyhistidine tails; protein immobilization

Indexed keywords

BACTERIA; CHELATION; CHROMATOGRAPHIC ANALYSIS; ENZYME IMMOBILIZATION; ENZYMES; GENES; GENETIC ENGINEERING; METALS; OLIGOMERS; ORGANIC ACIDS; PRECIPITATION (CHEMICAL); SOLUTIONS;

EID: 15844412754     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19960720)51:2<221::AID-BIT12>3.0.CO;2-P     Document Type: Article
Times cited : (29)

References (23)
  • 1
    • 0026071781 scopus 로고
    • Metal-affinity separations: A new dimension in protein processing
    • Arnold, F. H. 1991. Metal-affinity separations: a new dimension in protein processing. Bio/Technology 9: 151-156.
    • (1991) Bio/Technology , vol.9 , pp. 151-156
    • Arnold, F.H.1
  • 2
    • 0019836423 scopus 로고
    • Expression of Pseudomonas fluorescens D-galactose dehydrogenase in E. coli
    • Buckel, P., Zehelein, E. 1981. Expression of Pseudomonas fluorescens D-galactose dehydrogenase in E. coli. Gene 16: 149-159.
    • (1981) Gene , vol.16 , pp. 149-159
    • Buckel, P.1    Zehelein, E.2
  • 3
    • 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. 1991. 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: 125-129.
    • (1991) Gene , vol.109 , pp. 125-129
    • Bülow, L.1    Mosbach, K.2
  • 5
    • 0011187255 scopus 로고
    • Bioassay for transactivation using human immunodeficiency virus tat-encoded protein
    • Gentz, R., Chen, C.-H., Rosen, C. A. 1989. Bioassay for transactivation using human immunodeficiency virus tat-encoded protein: Proc. Natl. Acad. Sci. USA 86: 821-824.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 821-824
    • Gentz, R.1    Chen, C.-H.2    Rosen, C.A.3
  • 6
    • 0023781763 scopus 로고
    • Genetic approach to facilitate purification of recombinant proteins with novel metal chelate absorbent
    • Hochuli, E., Bannwarth, W., Doebeli, H., Gentz, R., Stueber, D. 1988. Genetic approach to facilitate purification of recombinant proteins with novel metal chelate absorbent. Bio/Technology 6: 1321-1325.
    • (1988) Bio/Technology , vol.6 , pp. 1321-1325
    • Hochuli, E.1    Bannwarth, W.2    Doebeli, H.3    Gentz, R.4    Stueber, D.5
  • 7
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 0018790602 scopus 로고
    • Affinity precipitation of enzymes
    • Larsson, P.-O., Mosbach, K. 1979. Affinity precipitation of enzymes. FEBS Lett. 98: 333-338.
    • (1979) FEBS Lett. , vol.98 , pp. 333-338
    • Larsson, P.-O.1    Mosbach, K.2
  • 9
    • 0025782267 scopus 로고
    • Metal affinity precipitation of proteins carrying genetically attached polyhistidine tails
    • Lilius, G., Persson, M., Bülow, L., Mosbach, K. 1991. Metal affinity precipitation of proteins carrying genetically attached polyhistidine tails. Eur. J. Biochem. 198: 499-504.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 499-504
    • Lilius, G.1    Persson, M.2    Bülow, L.3    Mosbach, K.4
  • 10
    • 0024841821 scopus 로고
    • Immobilization and affinity purification of recombinant proteins using histidine peptide fusions
    • Ljungquist, C., Breitholtz, Brink-Nilsson, H., Moks, T., Uhlén, M., Nilsson, B., 1989. Immobilization and affinity purification of recombinant proteins using histidine peptide fusions. Eur. J. Biochem. 186: 563-569.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 563-569
    • Ljungquist, C.1    Breitholtz2    Brink-Nilsson, H.3    Moks, T.4    Uhlén, M.5    Nilsson, B.6
  • 11
    • 0026576660 scopus 로고
    • Immobilization of monoclonal antibodies for affinity chromatography using a chelating peptide
    • Loethscher, P., Mottlau, L., Hochuli, E. 1992. Immobilization of monoclonal antibodies for affinity chromatography using a chelating peptide. J. Chromatogr. 595: 113-119.
    • (1992) J. Chromatogr. , vol.595 , pp. 113-119
    • Loethscher, P.1    Mottlau, L.2    Hochuli, E.3
  • 12
    • 0005508224 scopus 로고
    • Immobilized enzymes and cells
    • Academic Press, Orlando, FL
    • Mosbach, K. (ed.) 1987. Immobilized enzymes and cells. Methods in Enzymology, 136. Academic Press, Orlando, FL.
    • (1987) Methods in Enzymology , pp. 136
    • Mosbach, K.1
  • 13
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath, J., Carlsson, J., Olsson, I., Belfrage, G. 1975. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258: 598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 14
    • 0019468616 scopus 로고
    • pUR 222, a vector for cloning and rapid chemical sequencing
    • Rüther, U., Koenen, M., Otto, K., Müller-Hill, B. 1981. pUR 222, a vector for cloning and rapid chemical sequencing. Nucl. Acids.Res. 9: 4087-4098.
    • (1981) Nucl. Acids.Res. , vol.9 , pp. 4087-4098
    • Rüther, U.1    Koenen, M.2    Otto, K.3    Müller-Hill, B.4
  • 16
    • 0025420050 scopus 로고
    • Engineering proteins for purification
    • Sassenfeld, H. M. 1990. Engineering proteins for purification. TIBTECH 8: 88-93.
    • (1990) TIBTECH , vol.8 , pp. 88-93
    • Sassenfeld, H.M.1
  • 17
    • 0018361393 scopus 로고
    • Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria
    • Schär, H.-P., Zuber, H. 1979. Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. Hoppe-Seyler's Z. Physiol. Chem. 360: 795-807.
    • (1979) Hoppe-Seyler's Z. Physiol. Chem. , vol.360 , pp. 795-807
    • Schär, H.-P.1    Zuber, H.2
  • 18
    • 0024296676 scopus 로고
    • Chelating peptide-immobilized metal ion affinity chromatography
    • Smith, M. C., Furman, T. C., Ingolia, T. D., Pidgeon, C. 1988. Chelating peptide-immobilized metal ion affinity chromatography. J. Biol. Chem. 263: 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
  • 19
    • 0025405524 scopus 로고
    • A mathematical model for metal affinity protein partioning
    • Suh, S.-S., Arnold, F. H. 1990. A mathematical model for metal affinity protein partioning. Biotechnol. Bioeng. 35: 682-690.
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 682-690
    • Suh, S.-S.1    Arnold, F.H.2
  • 20
    • 0021967194 scopus 로고
    • Purification of proteins by IMAC
    • Sulkowski, E. 1985. Purification of proteins by IMAC. TIBTECH 3: 1-7.
    • (1985) TIBTECH , vol.3 , pp. 1-7
    • Sulkowski, E.1
  • 23
    • 0026391951 scopus 로고
    • Immobilized metal ion affinity chromatography (IMAC) - Chemistry and bioseparation
    • Wong, J. W., Albright, R. L., Wang, N.-H. L. 1991. Immobilized metal ion affinity chromatography (IMAC) - chemistry and bioseparation. Sep. Purif. Meth. 20: 49-106.
    • (1991) Sep. Purif. Meth. , vol.20 , pp. 49-106
    • Wong, J.W.1    Albright, R.L.2    Wang, N.-H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.