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Volumn 51, Issue 5, 2010, Pages 1128-1133

Novel approaches using alkaline or acid/guanidine treatment to eliminate therapeutic antibody interference in the measurement of total target ligand

Author keywords

Acid guanidine dissociation; Alkaline dissociation; Duplex immunoassay; Ligand binding assay; Therapeutic interference; Total target measurement

Indexed keywords

ALKALINE EARTH METAL; BUFFER; GUANIDINE; LIGAND; MONOCLONAL ANTIBODY; PROTEIN;

EID: 72749084561     PISSN: 07317085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpba.2009.11.021     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • Roopenian D.C., and Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol. 7 (2007) 715-725
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 2
    • 65249119387 scopus 로고    scopus 로고
    • Dose-dependent increases in circulating TGF-α and other EGFR ligands act as pharmacodynamic markers for optimal biological dosing of cetuximab and are tumor independent
    • Mutsaers A.J., Francia G., Man S., Lee C.R., Ebos J.M.L., Wu Y., Witte L., Berry S., Moore M., and Kerbel R.S. Dose-dependent increases in circulating TGF-α and other EGFR ligands act as pharmacodynamic markers for optimal biological dosing of cetuximab and are tumor independent. Clin. Cancer Res. 15 (2009) 2397-2405
    • (2009) Clin. Cancer Res. , vol.15 , pp. 2397-2405
    • Mutsaers, A.J.1    Francia, G.2    Man, S.3    Lee, C.R.4    Ebos, J.M.L.5    Wu, Y.6    Witte, L.7    Berry, S.8    Moore, M.9    Kerbel, R.S.10
  • 3
    • 8644234910 scopus 로고    scopus 로고
    • Antibody pharmacokinetics and pharmacodynamics
    • Lobo E.D., Hansen R.J., and Balthasar J.P. Antibody pharmacokinetics and pharmacodynamics. J. Pharm. Sci. 93 (2004) 2645-2668
    • (2004) J. Pharm. Sci. , vol.93 , pp. 2645-2668
    • Lobo, E.D.1    Hansen, R.J.2    Balthasar, J.P.3
  • 4
    • 72749117189 scopus 로고    scopus 로고
    • A mechanism based binding model for the population pharmacokinetics and pharmacodynamics of canakinumab, a monoclonal antibody in development for rheumatoid arthritis
    • Atlanta, GA
    • S. Tannebaum, A. Gautier, P. Lowe, A mechanism based binding model for the population pharmacokinetics and pharmacodynamics of canakinumab, a monoclonal antibody in development for rheumatoid arthritis, 2008 AAPS Annual Meeting. Atlanta, GA, www.aapsj.org/abstracts/AM_2008/AAPS2008-002581.PDF.
    • (2008) AAPS Annual Meeting
    • Tannebaum, S.1    Gautier, A.2    Lowe, P.3
  • 5
    • 34247344172 scopus 로고    scopus 로고
    • A mechanism-based binding model for the population pharmacokinetics and pharmacodynamics of omalizumab
    • Hayashi N., Tsukamoto Y., Sallas W.M., and Lowe P.J. A mechanism-based binding model for the population pharmacokinetics and pharmacodynamics of omalizumab. Br. J. Clin. Pharmacol. 63 (2006) 548-561
    • (2006) Br. J. Clin. Pharmacol. , vol.63 , pp. 548-561
    • Hayashi, N.1    Tsukamoto, Y.2    Sallas, W.M.3    Lowe, P.J.4
  • 6
    • 34249277443 scopus 로고    scopus 로고
    • Key elements of bioanalytical method validation for macromolecules
    • Kelly M., and DeSilva B. Key elements of bioanalytical method validation for macromolecules. AAPS J. 9 (2007) E156-E163
    • (2007) AAPS J. , vol.9
    • Kelly, M.1    DeSilva, B.2
  • 7
    • 34250675994 scopus 로고    scopus 로고
    • Specificity and selectivity evaluations of ligand binding assay of protein therapeutics against concomitant drugs and related endogenous proteins
    • Lee J., and Ma H. Specificity and selectivity evaluations of ligand binding assay of protein therapeutics against concomitant drugs and related endogenous proteins. AAPS J. 9 (2007) E164-E170
    • (2007) AAPS J. , vol.9
    • Lee, J.1    Ma, H.2
  • 9
    • 53049093562 scopus 로고    scopus 로고
    • A novel method for quantitative measurement of a biomarker in the presence of a therapeutic monoclonal antibody directed against the biomarker
    • Davis R.A., Butterfiled A.M., Konard R.J., and Bourdage J.S. A novel method for quantitative measurement of a biomarker in the presence of a therapeutic monoclonal antibody directed against the biomarker. J. Pharm. Biomed. Anal. 48 (2008) 897-901
    • (2008) J. Pharm. Biomed. Anal. , vol.48 , pp. 897-901
    • Davis, R.A.1    Butterfiled, A.M.2    Konard, R.J.3    Bourdage, J.S.4
  • 11
    • 0031081605 scopus 로고    scopus 로고
    • pH-dependent isoform transitions of a monoclonal antibody monitored by micellar electrokinetic capillary chromatography
    • Kats M., Richberg P.C., and Hughes D.E. pH-dependent isoform transitions of a monoclonal antibody monitored by micellar electrokinetic capillary chromatography. Anal. Chem. 69 (1997) 338-343
    • (1997) Anal. Chem. , vol.69 , pp. 338-343
    • Kats, M.1    Richberg, P.C.2    Hughes, D.E.3
  • 12
    • 0014145446 scopus 로고
    • Dissociation of low density lipoprotein-antibody precipitates at alkaline pH
    • Chung J., and Nishida T. Dissociation of low density lipoprotein-antibody precipitates at alkaline pH. J. Lipid Res. 8 (1967) 631-635
    • (1967) J. Lipid Res. , vol.8 , pp. 631-635
    • Chung, J.1    Nishida, T.2
  • 13
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein
    • Vermeer A.W.P., and 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
  • 14
    • 0037317890 scopus 로고    scopus 로고
    • Small, acid-soluble proteins as biomarkers in mass spectrometry analysis of Bacillus spores
    • Hathout Y., Setlow B., Martinez R.-M.C., Fenselau C., and Setlow P. Small, acid-soluble proteins as biomarkers in mass spectrometry analysis of Bacillus spores. Appl. Environ. Microbiol. 69 (2003) 1100-1107
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1100-1107
    • Hathout, Y.1    Setlow, B.2    Martinez, R.-M.C.3    Fenselau, C.4    Setlow, P.5
  • 15
    • 26844566629 scopus 로고    scopus 로고
    • Uncovering the unfoldome: enriching cell extracts for unstructured proteins by acid treatment
    • Cortese M.S., Baird J.P., Uversky V.N., and Dunker A.K. Uncovering the unfoldome: enriching cell extracts for unstructured proteins by acid treatment. J. Proteome Res. 4 (2005) 1610-1618
    • (2005) J. Proteome Res. , vol.4 , pp. 1610-1618
    • Cortese, M.S.1    Baird, J.P.2    Uversky, V.N.3    Dunker, A.K.4
  • 16
    • 0017652251 scopus 로고
    • Studies on human placental alkaline phosphatase purification by immunoabsorption and comparison of the "A" and "B" forms of the enzyme
    • Doellgast G.J., Spiegel J., Guenther R.A., and Fishman W.H. Studies on human placental alkaline phosphatase purification by immunoabsorption and comparison of the "A" and "B" forms of the enzyme. Biochim. Biophys. Acta 484 (1977) 59-78
    • (1977) Biochim. Biophys. Acta , vol.484 , pp. 59-78
    • Doellgast, G.J.1    Spiegel, J.2    Guenther, R.A.3    Fishman, W.H.4
  • 17
    • 0019520495 scopus 로고
    • Acid-soluble spore proteins of Bacillus subtilis
    • Johnson W.C., and Tipper D.J. Acid-soluble spore proteins of Bacillus subtilis. J. Bacteriol. 146 (1981) 972-982
    • (1981) J. Bacteriol. , vol.146 , pp. 972-982
    • Johnson, W.C.1    Tipper, D.J.2
  • 18
    • 0001407358 scopus 로고
    • Conformational changes and functional properties of acid-modified soy protein
    • Matsudomi N., Sasaki T., Kato A., and Kobayashi K. Conformational changes and functional properties of acid-modified soy protein. Agric. Biol. Chem. 49 (1985) 1251-1256
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 1251-1256
    • Matsudomi, N.1    Sasaki, T.2    Kato, A.3    Kobayashi, K.4
  • 19
    • 0024212295 scopus 로고
    • Failure of acid-ethanol treatment to prevent interference by binding proteins in radioligand assays for the insulin-like growth factors
    • Mesiano S., Young I.R., Browne C.A., and Thorburn G.D. Failure of acid-ethanol treatment to prevent interference by binding proteins in radioligand assays for the insulin-like growth factors. J. Endocrinol. 119 (1988) 453-460
    • (1988) J. Endocrinol. , vol.119 , pp. 453-460
    • Mesiano, S.1    Young, I.R.2    Browne, C.A.3    Thorburn, G.D.4
  • 20
    • 24344448252 scopus 로고    scopus 로고
    • An acid dissociation bridging ELISA for detection of antibodies directed against therapeutic proteins in the presence of antigen
    • Patton A., Mullenix M.C., Swanson S.J., and Koren E. An acid dissociation bridging ELISA for detection of antibodies directed against therapeutic proteins in the presence of antigen. J. Immunol. Methods 304 (2005) 189-195
    • (2005) J. Immunol. Methods , vol.304 , pp. 189-195
    • Patton, A.1    Mullenix, M.C.2    Swanson, S.J.3    Koren, E.4
  • 21
    • 0018168063 scopus 로고
    • Purification and characterization of additional low-molecular-weight basic proteins degraded during germination of Bacillus megaterium spores
    • Setlow P. Purification and characterization of additional low-molecular-weight basic proteins degraded during germination of Bacillus megaterium spores. J. Bacteriol. 136 (1978) 331-340
    • (1978) J. Bacteriol. , vol.136 , pp. 331-340
    • Setlow, P.1
  • 22
    • 0015937407 scopus 로고
    • Structural alterations of acidic proteins by acid treatment of chromatin
    • Spelsberg T.C., Mitchell W.M., and Chytil F. Structural alterations of acidic proteins by acid treatment of chromatin. Mol. Cell. Biochem. 1 (1973) 243-251
    • (1973) Mol. Cell. Biochem. , vol.1 , pp. 243-251
    • Spelsberg, T.C.1    Mitchell, W.M.2    Chytil, F.3
  • 23
    • 0037069399 scopus 로고    scopus 로고
    • Protein stabilization by urea and guanidine hydrochloride
    • Bhuyan A.K. Protein stabilization by urea and guanidine hydrochloride. Biochemistry 41 (2002) 13386-13394
    • (2002) Biochemistry , vol.41 , pp. 13386-13394
    • Bhuyan, A.K.1
  • 25
    • 0013789790 scopus 로고
    • Dissociation of human CO-hemoglobin by urea, guanidine hydrochloride, and other reagents
    • Kawahara K., Kirshner A.G., and Tanford C. Dissociation of human CO-hemoglobin by urea, guanidine hydrochloride, and other reagents. Biochemistry 4 (1965) 1203-1213
    • (1965) Biochemistry , vol.4 , pp. 1203-1213
    • Kawahara, K.1    Kirshner, A.G.2    Tanford, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.