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Volumn 36, Issue 2, 2004, Pages 244-248

Elution of antibodies from a Protein-A column by aqueous arginine solutions

Author keywords

Antibody purification; Arginine; Elution; Protein A

Indexed keywords

ARGININE; BACTERIAL PROTEIN; CITRIC ACID; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; STAPHYLOCOCCUS PROTEIN A;

EID: 3142537435     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.04.009     Document Type: Article
Times cited : (180)

References (28)
  • 1
    • 0348098872 scopus 로고    scopus 로고
    • Performance comparison of protein a affinity-chromatography sorbents for purifying recombinant monoclonal antibodies
    • Fahrner R.L., Whitney D.H., Vanderlaan M., Blank G.S. Performance comparison of protein A affinity-chromatography sorbents for purifying recombinant monoclonal antibodies. Biotechnol. Appl. Biochem. 30:1999;121-128
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 121-128
    • Fahrner, R.L.1    Whitney, D.H.2    Vanderlaan, M.3    Blank, G.S.4
  • 3
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer A.W.P., Norde W. The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein. Biophys. J. 78:2000;394-404
    • (2000) Biophys. J. , vol.78 , pp. 394-404
    • Vermeer, A.W.P.1    Norde, W.2
  • 4
    • 0001223962 scopus 로고    scopus 로고
    • Non-native conformational states of immunoglobulins: Thermodynamic and functional studies of rabbit IgG
    • Vlasov A.P., Kravchuk Z.I., Martsev S.P. Non-native conformational states of immunoglobulins: thermodynamic and functional studies of rabbit IgG. Biochemistry (Moscow). 61:1996;155-171
    • (1996) Biochemistry (Moscow) , vol.61 , pp. 155-171
    • Vlasov, A.P.1    Kravchuk, Z.I.2    Martsev, S.P.3
  • 5
    • 0028916303 scopus 로고
    • Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH-induced state
    • Martsev S.P., Kravchuk Z.I., Vlasov A.P., Lyakhnovich G.V. Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH-induced state. FEBS Lett. 361:1995;173-175
    • (1995) FEBS Lett. , vol.361 , pp. 173-175
    • Martsev, S.P.1    Kravchuk, Z.I.2    Vlasov, A.P.3    Lyakhnovich, G.V.4
  • 6
    • 0026332693 scopus 로고
    • Temperature and pH dependence of immunoglobulin G conformation
    • Calmettes P., Cser L., Rajnavolgyi E. Temperature and pH dependence of immunoglobulin G conformation. Arch. Biochem. Biophys. 291:1991;277-283
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 277-283
    • Calmettes, P.1    Cser, L.2    Rajnavolgyi, E.3
  • 7
    • 0025837548 scopus 로고
    • Alternatively folded states of an immunoglobulin
    • Buchner J., Renner M.R., Lilie H., et al. Alternatively folded states of an immunoglobulin. Biochemistry. 30:1991;6922-6929
    • (1991) Biochemistry , vol.30 , pp. 6922-6929
    • Buchner, J.1    Renner, M.R.2    Lilie, H.3
  • 9
    • 0032940238 scopus 로고    scopus 로고
    • Conformation, pH-induced conformational change, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments
    • Welfle K., Misselwitz R., Hausdorf G., Hohne W., Welfle H. Conformation, pH-induced conformational change, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments. Biochim. Biophys. Acta. 1431:1999;120-131
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 120-131
    • Welfle, K.1    Misselwitz, R.2    Hausdorf, G.3    Hohne, W.4    Welfle, H.5
  • 10
    • 0028605960 scopus 로고
    • Large increase in thermal stability of CH2 domain of rabbit IgG after acid treatment as evidenced by differential scanning calorimetry
    • Martsev S.P., Kravchuk Z.I., Vlasov A.P. Large increase in thermal stability of CH2 domain of rabbit IgG after acid treatment as evidenced by differential scanning calorimetry. Immunol. Lett. 43:1994;149-152
    • (1994) Immunol. Lett. , vol.43 , pp. 149-152
    • Martsev, S.P.1    Kravchuk, Z.I.2    Vlasov, A.P.3
  • 11
    • 0032703669 scopus 로고    scopus 로고
    • Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying
    • Sarciax J.M., Mansour S., Hageman M.J., Nail S.L. Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying. J. Pharm. Sci. 88:1999;1354-1361
    • (1999) J. Pharm. Sci. , vol.88 , pp. 1354-1361
    • Sarciax, J.M.1    Mansour, S.2    Hageman, M.J.3    Nail, S.L.4
  • 12
    • 0028300715 scopus 로고
    • Chemical and physical stability of chimeric L6, a mouse-human monoclonal antibody
    • Paborji M., Pochopin N.L., Coppola W.P., Bogardus J.B. Chemical and physical stability of chimeric L6, a mouse-human monoclonal antibody. Pharm. Res. 11:1994;764-771
    • (1994) Pharm. Res. , vol.11 , pp. 764-771
    • Paborji, M.1    Pochopin, N.L.2    Coppola, W.P.3    Bogardus, J.B.4
  • 15
    • 0024295583 scopus 로고
    • Rapid high-performance affinity chromatography on micropellicular sorbents
    • Varady L., Kalghatgi K., Horvath C. Rapid high-performance affinity chromatography on micropellicular sorbents. J. Chromatogr. 458:1988;207-215
    • (1988) J. Chromatogr. , vol.458 , pp. 207-215
    • Varady, L.1    Kalghatgi, K.2    Horvath, C.3
  • 16
    • 0019362118 scopus 로고
    • Isolation of circulating immune complexes by conglutinin and separation of antigen from dissociated complexes by immobilized protein a
    • Gupta R.C., Tan E.M. Isolation of circulating immune complexes by conglutinin and separation of antigen from dissociated complexes by immobilized protein A. Clin. Exp. Immunol. 46:1981;9-19
    • (1981) Clin. Exp. Immunol. , vol.46 , pp. 9-19
    • Gupta, R.C.1    Tan, E.M.2
  • 17
    • 0345045570 scopus 로고    scopus 로고
    • Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatography
    • Gulich S., Uhlen M., Hober S. Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatography. J. Biotechnol. 76:2000;233-244
    • (2000) J. Biotechnol. , vol.76 , pp. 233-244
    • Gulich, S.1    Uhlen, M.2    Hober, S.3
  • 18
    • 0037146780 scopus 로고    scopus 로고
    • Affinity purification of polyclonal antibodies using a new all-D synthetic peptide ligand: Comparison with protein a and protein G
    • Verdoliva A., Pannone F., Rossi M., Catello S., Manfredi V. Affinity purification of polyclonal antibodies using a new all-D synthetic peptide ligand: comparison with protein A and protein G. J. Immunol. Methods. 271:2002;77-88
    • (2002) J. Immunol. Methods , vol.271 , pp. 77-88
    • Verdoliva, A.1    Pannone, F.2    Rossi, M.3    Catello, S.4    Manfredi, V.5
  • 20
    • 0031717907 scopus 로고    scopus 로고
    • A study of the interactions between an IgG-binding domain based on the B domain of staphylococcal protein a and rabbit IgG
    • Brown N.L., Bottomley S.P., Scawen M.D., Gore M.G. A study of the interactions between an IgG-binding domain based on the B domain of staphylococcal protein A and rabbit IgG. Mol. Biotechnol. 10:1998;9-16
    • (1998) Mol. Biotechnol. , vol.10 , pp. 9-16
    • Brown, N.L.1    Bottomley, S.P.2    Scawen, M.D.3    Gore, M.G.4
  • 21
    • 0036680280 scopus 로고    scopus 로고
    • Antibody separation by hydrophobic charge induction chromatography
    • Boschetti E. Antibody separation by hydrophobic charge induction chromatography. Trends Biotechnol. 20:2002;333-337
    • (2002) Trends Biotechnol. , vol.20 , pp. 333-337
    • Boschetti, E.1
  • 22
    • 0026510381 scopus 로고
    • Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: Influence of interdomain connections
    • Brinkmann U., Buchner J., Pastan I. Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: influence of interdomain connections. Proc. Natl. Acad. Sci. USA. 89:1992;3075-3079
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3075-3079
    • Brinkmann, U.1    Buchner, J.2    Pastan, I.3
  • 23
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner J., Rudolph R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio/Technology. 9:1991;157-162
    • (1991) Bio/Technology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 24
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies
    • Arora D., Khanna N.J. Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies. J. Biotechnol. 52:1996;127-133
    • (1996) J. Biotechnol. , vol.52 , pp. 127-133
    • Arora, D.1    Khanna, N.J.2
  • 25
    • 0036774673 scopus 로고    scopus 로고
    • Biophysical effect of amino acids on the prevention of protein aggregation
    • Shiraki K., Kudou M., Fujiwara S., Imanaka T., Takagi M. Biophysical effect of amino acids on the prevention of protein aggregation. J. Biochem. 132:2002;591-595
    • (2002) J. Biochem. , vol.132 , pp. 591-595
    • Shiraki, K.1    Kudou, M.2    Fujiwara, S.3    Imanaka, T.4    Takagi, M.5
  • 26
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • Arakawa T., Tsumoto K. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304:2003;148-152
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 27
    • 0345636051 scopus 로고    scopus 로고
    • Practical considerations in refolding proteins from inclusion bodies
    • Tsumoto K., Ejima D., Kumagai I., Arakawa T. Practical considerations in refolding proteins from inclusion bodies. Protein Expr. Purif. 28:2003;1-8
    • (2003) Protein Expr. Purif. , vol.28 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4
  • 28
    • 0344495223 scopus 로고    scopus 로고
    • Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine
    • Tsumoto K., Umetsu M., Kumagai I., Ejima D., Arakawa T. Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem. Biophys. Res. Commun. 312:2003;1383-1386
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1383-1386
    • Tsumoto, K.1    Umetsu, M.2    Kumagai, I.3    Ejima, D.4    Arakawa, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.