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Volumn 19, Issue 4, 2006, Pages 340-347

Screening of suitable immobilized metal chelates for adsorption of monoclonal antibodies against mutant amidase from Pseudomonas aeruginosa

Author keywords

Altered (T103I) amidase; Co2+ ions; Epichlorohydrin; IgM class; Immobilized metal affinity chromatography; Monoclonal antibodies; Pseudomonas aeruginosa

Indexed keywords

AMIDASE; CHELATING AGENT; IMIDAZOLE; IMIDAZOLE DERIVATIVE; IMMUNOGLOBULIN M; METAL; MONOCLONAL ANTIBODY;

EID: 33747324824     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.773     Document Type: Conference Paper
Times cited : (13)

References (27)
  • 2
    • 0026071781 scopus 로고
    • Metal-affinity separations: A new dimension in protein processing
    • Arnold FH. 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
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 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
  • 4
    • 0015328697 scopus 로고
    • Amino acid susbtitution in an amidase produced by an acetanilide- utilizing mutant of Pseudomonas aeruginosa
    • Brown PR, Clarke PH. 1972. Amino acid susbtitution in an amidase produced by an acetanilide-utilizing mutant of Pseudomonas aeruginosa. J. Gen. Microbiol. 70: 287-298.
    • (1972) J. Gen. Microbiol. , vol.70 , pp. 287-298
    • Brown, P.R.1    Clarke, P.H.2
  • 5
    • 0035975882 scopus 로고    scopus 로고
    • Twenty-five years of immobilized metal ion affinity chromatography: Past, present and future
    • Chaga GS. 2001. Twenty-five years of immobilized metal ion affinity chromatography: past, present and future. J. Biochem. Biophys. Methods. 49: 313-334.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 313-334
    • Chaga, G.S.1
  • 6
    • 0035975923 scopus 로고    scopus 로고
    • Perspectives of immobilized-metal affinity chromatography
    • Gaberc-Porekar V, Menart V. 2001. Perspectives of immobilized-metal affinity chromatography. J. Biochem. Biophys. Methods 49, 335-360.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 335-360
    • Gaberc-Porekar, V.1    Menart, V.2
  • 7
    • 0027971005 scopus 로고
    • Purification of humanized murine and murine monoclonal antibodies using immobilized metal affinity chromatography
    • Hale JE, Beidler DE. 1994. Purification of humanized murine and murine monoclonal antibodies using immobilized metal affinity chromatography. Anal. Biochem. 222: 29-33.
    • (1994) Anal. Biochem. , vol.222 , pp. 29-33
    • Hale, J.E.1    Beidler, D.E.2
  • 8
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis
    • Hames BD, Rickwood D (eds). IRL Press: Oxford
    • Hames BD. 1981. An introduction to polyacrylamide gel electrophoresis. In Gel Electrophoresis of Proteins, Hames BD, Rickwood D (eds). IRL Press: Oxford; 1-86.
    • (1981) Gel Electrophoresis of Proteins , pp. 1-86
    • Hames, B.D.1
  • 9
    • 0028978254 scopus 로고
    • Importance of the α-amino group in the selective purification of synthetic histidine peptides by immobilised metal ion affinity chromatography
    • Hansen P, Lindeberg G. 1995. Importance of the α-amino group in the selective purification of synthetic histidine peptides by immobilised metal ion affinity chromatography. J. Chromatogr. A. 690: 155-159.
    • (1995) J. Chromatogr. A , vol.690 , pp. 155-159
    • Hansen, P.1    Lindeberg, G.2
  • 10
    • 0000013959 scopus 로고
    • Immunoassays
    • Johnstone A, Thorpe R (eds). Blackwell Scientific Publications: Oxford
    • Johnstone A, Thorpe R. 1987. Immunoassays. In Immunochemistry in Practice, Johnstone A, Thorpe R (eds). Blackwell Scientific Publications: Oxford; 257-260.
    • (1987) Immunochemistry in Practice , pp. 257-260
    • Johnstone, A.1    Thorpe, R.2
  • 11
    • 0034966202 scopus 로고    scopus 로고
    • Substitutions of Thr-103-Ile and TRP-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetic properties and enzyme instability
    • Karmali A, Pacheco R, Tata R, Brown PR. 2001. Substitutions of Thr-103-Ile and TRP-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetic properties and enzyme instability. Mol. Biotechnol. 17: 201-212.
    • (2001) Mol. Biotechnol. , vol.17 , pp. 201-212
    • Karmali, A.1    Pacheco, R.2    Tata, R.3    Brown, P.R.4
  • 12
    • 0033744551 scopus 로고    scopus 로고
    • Substitution of Glu-59 by Val in amidase from Pseudomonas aeruginosa results in a catalytically inactive enzyme
    • Karmali A, Tata R, Brown PR. 2000. Substitution of Glu-59 by Val in amidase from Pseudomonas aeruginosa results in a catalytically inactive enzyme. Mol. Biotechnol. 16: 5-16.
    • (2000) Mol. Biotechnol. , vol.16 , pp. 5-16
    • Karmali, A.1    Tata, R.2    Brown, P.R.3
  • 13
    • 0344494027 scopus 로고    scopus 로고
    • Applications of affinity chromatography in proteomics
    • Lee W-C, Lee KH. 2004. Applications of affinity chromatography in proteomics. Anal. Biochem. 324: 1-10.
    • (2004) Anal. Biochem. , vol.324 , pp. 1-10
    • Lee, W.-C.1    Lee, K.H.2
  • 14
    • 24644434377 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies against mutant amidase from Pseudomonas aeruginosa
    • Martins S, Karmali A, Andrade J, Custódio A, Serralheiro ML. 2005. Characterization of monoclonal antibodies against mutant amidase from Pseudomonas aeruginosa. Mol. Biotechnol. 30: 207-219.
    • (2005) Mol. Biotechnol. , vol.30 , pp. 207-219
    • Martins, S.1    Karmali, A.2    Andrade, J.3    Custódio, A.4    Serralheiro, M.L.5
  • 15
    • 0035975883 scopus 로고    scopus 로고
    • The solid phase in affinity chromatography: Strategies for antibody attachment
    • Nisnevitch M, Firer MA. 2001. The solid phase in affinity chromatography: strategies for antibody attachment. J. Biochem. Biophys. Methods. 49: 467-480.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 467-480
    • Nisnevitch, M.1    Firer, M.A.2
  • 16
    • 0034766855 scopus 로고    scopus 로고
    • A monoclonal antibody specific for Pseudomonas aeruginosa amidase
    • Novo C, Karmali A, Clemente A, Brown PR. 2001. A monoclonal antibody specific for Pseudomonas aeruginosa amidase. Hybridoma 20: 273-279.
    • (2001) Hybridoma , vol.20 , pp. 273-279
    • Novo, C.1    Karmali, A.2    Clemente, A.3    Brown, P.R.4
  • 17
    • 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
  • 18
    • 0026910385 scopus 로고
    • Immobilized metal ion affinity chromatography
    • Porath J. 1992. Immobilized metal ion affinity chromatography. Protein Expr. Purif. 3: 263-281.
    • (1992) Protein Expr. Purif. , vol.3 , pp. 263-281
    • Porath, J.1
  • 19
    • 0021967194 scopus 로고
    • Purification of proteins by IMAC
    • Sulkowski E. 1985. Purification of proteins by IMAC. Trends Biotechnol. 3: 1-7.
    • (1985) Trends Biotechnol. , vol.3 , pp. 1-7
    • Sulkowski, E.1
  • 21
    • 0028157408 scopus 로고
    • Multiple-site binding interactions in metal-affinity chromatography. I - Equilibrium binding of engineered histidine-containing cytochromes c
    • Todd RJ, Johnson D, Arnold FH. 1994. Multiple-site binding interactions in metal-affinity chromatography. I - Equilibrium binding of engineered histidine-containing cytochromes c. J. Chromatography A. 662: 13-26.
    • (1994) J. Chromatography A , vol.662 , pp. 13-26
    • Todd, R.J.1    Johnson, D.2    Arnold, F.H.3
  • 23
    • 0347613015 scopus 로고    scopus 로고
    • Current and prospective applications of metal ion-protein binding
    • Ueda EKM, Gout PW, Morganti L. 2003. Current and prospective applications of metal ion-protein binding. J. Chromatography A. 988: 1-23.
    • (2003) J. Chromatography A , vol.988 , pp. 1-23
    • Ueda, E.K.M.1    Gout, P.W.2    Morganti, L.3
  • 25
    • 0028420790 scopus 로고
    • Immobilized metal ion affinity chromatography
    • Yip TT, Hutchens TW. 1994. Immobilized metal ion affinity chromatography. Mol. Biotechnol. 1: 151-164.
    • (1994) Mol. Biotechnol. , vol.1 , pp. 151-164
    • Yip, T.T.1    Hutchens, T.W.2
  • 26
    • 0029116927 scopus 로고
    • Protein selectivity in immobilized metal affinity chromatography based on the surface accessibility of aspartic and glutamic acid residues
    • Zachariou M, Hearn MT. 1995. Protein selectivity in immobilized metal affinity chromatography based on the surface accessibility of aspartic and glutamic acid residues. J. Protein Chem. 14: 419-430.
    • (1995) J. Protein Chem. , vol.14 , pp. 419-430
    • Zachariou, M.1    Hearn, M.T.2
  • 27
    • 0030043946 scopus 로고    scopus 로고
    • Applications of immobilized metal ion chelate complexes as pseudocation exchange adsorbents for protein separation
    • Zachariou M, Hearn MT. 1996. Applications of immobilized metal ion chelate complexes as pseudocation exchange adsorbents for protein separation. Biochemistry 35: 202-211.
    • (1996) Biochemistry , vol.35 , pp. 202-211
    • Zachariou, M.1    Hearn, M.T.2


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