메뉴 건너뛰기




Volumn 5, Issue 2, 2013, Pages 227-244

Characterization of critical reagents in ligand-binding assays: Enabling robust bioanalytical methods and lifecycle management

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY C1414A; MONOCLONAL ANTIBODY C437A; REAGENT; UNCLASSIFIED DRUG;

EID: 84872967092     PISSN: 17576180     EISSN: 17576199     Source Type: Journal    
DOI: 10.4155/bio.12.304     Document Type: Review
Times cited : (46)

References (52)
  • 1
    • 84863930293 scopus 로고    scopus 로고
    • Pharmacokinetics and toxicology of therapeutic proteins: Advances and challenges
    • Vugmeyster Y, Xu X, Theil FP, Khawli LA, Leach Mw. Pharmacokinetics and toxicology of therapeutic proteins: Advances and challenges. World J. Biol. Chem. 3(4), 73-92 (2012).
    • (2012) World J. Biol. Chem , vol.3 , Issue.4 , pp. 73-92
    • Vugmeyster, Y.1    Xu, X.2    Theil, F.P.3    Khawli, L.A.4    Mw, L.5
  • 2
    • 33744950980 scopus 로고    scopus 로고
    • Scientific and regulatory considerations on the immunogenicity of biologics
    • DOI 10.1016/j.tibtech.2006.04.001, PII S0167779906000825
    • Shankar G, Shores E, Wagner C, Mire-Sluis A. Scientific and regulatory considerations on the immunogenicity of biologics. Trends Biotechnol. 24(6), 274-280 (2006). (Pubitemid 43853075)
    • (2006) Trends in Biotechnology , vol.24 , Issue.6 , pp. 274-280
    • Shankar, G.1    Shores, E.2    Wagner, C.3    Mire-Sluis, A.4
  • 3
    • 79952655910 scopus 로고    scopus 로고
    • Quality assessment of bioanalytical quantification of monoclonal antibody drugs
    • Lee JW, Kelley M. Quality assessment of bioanalytical quantification of monoclonal antibody drugs. Ther. Deliv. 2(3), 383-396 (2011).
    • (2011) Ther. Deliv , vol.2 , Issue.3 , pp. 383-396
    • Lee, J.W.1    Kelley, M.2
  • 4
    • 79953114938 scopus 로고    scopus 로고
    • Unique challenges of providing bioanalytical support for biological therapeutic pharmacokinetic programs
    • Nowatzke WL, Rogers K, Wells E, Bowsher RR, Ray C, Unger S. Unique challenges of providing bioanalytical support for biological therapeutic pharmacokinetic programs. Bioanalysis 3(5), 509-521 (2011).
    • (2011) Bioanalysis , vol.3 , Issue.5 , pp. 509-521
    • Nowatzke, W.L.1    Rogers, K.2    Wells, E.3    Bowsher, R.R.4    Ray, C.5    Unger, S.6
  • 5
    • 84860710411 scopus 로고    scopus 로고
    • Immunogenicity to therapeutic proteins: Impact on PK/PD and efficacy
    • Chirmule N, Jawa V, Meibohm B. Immunogenicity to therapeutic proteins: impact on PK/PD and efficacy. AAPS J. 14(2), 296-302 (2012).
    • (2012) AAPS J , vol.14 , Issue.2 , pp. 296-302
    • Chirmule, N.1    Jawa, V.2    Meibohm, B.3
  • 6
    • 79951980085 scopus 로고    scopus 로고
    • Bioanalytical approaches to quantify 'total' and 'free' therapeutic antibodies and their targets: Technical challenges and PK/PD applications over the course of drug development
    • Lee JW, Kelley M, King LE et al. Bioanalytical approaches to quantify 'total' and 'free' therapeutic antibodies and their targets: technical challenges and PK/PD applications over the course of drug development. AAPS J. 13(1), 99-110 (2011).
    • (2011) AAPS J , vol.13 , Issue.1 , pp. 99-110
    • Lee, J.W.1    Kelley, M.2    King, L.E.3
  • 7
    • 10744230729 scopus 로고    scopus 로고
    • Recommendations for the Bioanalytical Method Validation of Ligand-binding Assays to Support Pharmacokinetic Assessments of Macromolecules
    • DOI 10.1023/B:PHAM.0000003390.51761.3d
    • Desilva B, Smith W, Weiner R et al. Recommendations for the bioanalytical method validation of ligand-binding assays to support pharmacokinetic assessments of macromolecules. Pharm. Res. 20(11), 1885-1900 (2003). (Pubitemid 37449466)
    • (2003) Pharmaceutical Research , vol.20 , Issue.11 , pp. 1885-1900
    • Desilva, B.1    Smith, W.2    Weiner, R.3    Kelley, M.4    Smolec, J.5    Lee, B.6    Khan, M.7    Tacey, R.8    Hill, H.9    Celniker, A.10
  • 9
    • 58249116651 scopus 로고    scopus 로고
    • Recommendations for the validation of immunoassays used for detection of host antibodies against biotechnology products
    • Shankar G, Devanarayan V, Amaravadi L et al. Recommendations for the validation of immunoassays used for detection of host antibodies against biotechnology products. J. Pharm. Biomed. Anal. 48(5), 1267-1281 (2008).
    • (2008) J. Pharm. Biomed. Anal , vol.48 , Issue.5 , pp. 1267-1281
    • Shankar, G.1    Devanarayan, V.2    Amaravadi, L.3
  • 10
    • 84860720468 scopus 로고    scopus 로고
    • Ligand-binding assays in the 21st century laboratory: Recommendations for characterization and supply of critical reagents
    • O'hara DM, Theobald V, Egan AC et al. Ligand-binding assays in the 21st century laboratory: recommendations for characterization and supply of critical reagents. AAPS J. 14(2), 316-328 (2012).
    • (2012) AAPS J , vol.14 , Issue.2 , pp. 316-328
    • O'Hara, D.M.1    Theobald, V.2    Egan, A.C.3
  • 11
    • 79953113665 scopus 로고    scopus 로고
    • Quality requirements for critical assay reagents used in bioanalysis of therapeutic proteins: What bioanalysts should know about their reagents
    • Staack RF, Stracke JO, Stubenrauch K, Vogel R, Schleypen J, Papadimitriou A. Quality requirements for critical assay reagents used in bioanalysis of therapeutic proteins: what bioanalysts should know about their reagents. Bioanalysis 3(5), 523-534 (2011).
    • (2011) Bioanalysis , vol.3 , Issue.5 , pp. 523-534
    • Staack, R.F.1    Stracke, J.O.2    Stubenrauch, K.3    Vogel, R.4    Schleypen, J.5    Papadimitriou, A.6
  • 12
    • 8344224534 scopus 로고    scopus 로고
    • Characteristics biological products and assessing comparability following manufacturing changes
    • DOI 10.1038/nbt1030
    • Chirino AJ, Mire-Sluis A. Characterizing biological products and assessing comparability following manufacturing changes. Nat. Biotechnol. 22(11), 1383-1391 (2004). (Pubitemid 39482857)
    • (2004) Nature Biotechnology , vol.22 , Issue.11 , pp. 1383-1391
    • Chirino, A.J.1    Mire-Sluis, A.2
  • 13
    • 62749198591 scopus 로고    scopus 로고
    • Evaluation of an immunoassay for human-specific quantitation of therapeutic antibodies in serum samples from non-human primates
    • Stubenrauch K, Wessels U, Lenz H. Evaluation of an immunoassay for human-specific quantitation of therapeutic antibodies in serum samples from non-human primates. J. Pharm. Biomed. Anal. 49(4), 1003-1008 (2009).
    • (2009) J. Pharm. Biomed. Anal , vol.49 , Issue.4 , pp. 1003-1008
    • Stubenrauch, K.1    Wessels, U.2    Lenz, H.3
  • 14
    • 33747451721 scopus 로고    scopus 로고
    • Current and future issues in the manufacturing and development of monoclonal antibodies
    • DOI 10.1016/j.addr.2006.05.002, PII S0169409X06000901
    • Kozlowski S, Swann P. Current and future issues in the manufacturing and development of monoclonal antibodies. Adv. Drug Deliv. Rev. 58(5-6), 707-722 (2006). (Pubitemid 44255854)
    • (2006) Advanced Drug Delivery Reviews , vol.58 , Issue.5-6 , pp. 707-722
    • Kozlowski, S.1    Swann, P.2
  • 16
    • 67449119292 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability of protein pharmaceuticals
    • Sola RJ, Griebenow K. Effects of glycosylation on the stability of protein pharmaceuticals. J. Pharm. Sci. 98(4), 1223-1245 (2009).
    • (2009) J. Pharm. Sci , vol.98 , Issue.4 , pp. 1223-1245
    • Sola, R.J.1    Griebenow, K.2
  • 17
    • 81255197729 scopus 로고    scopus 로고
    • The impact of glycosylation on monoclonal antibody conformation and stability
    • Zheng K, Bantog C, Bayer R. The impact of glycosylation on monoclonal antibody conformation and stability. MAbs 3(6), 568-576 (2011).
    • (2011) MAbs , vol.3 , Issue.6 , pp. 568-576
    • Zheng, K.1    Bantog, C.2    Bayer, R.3
  • 18
    • 41149093491 scopus 로고    scopus 로고
    • Immunopurification and mass spectrometric quantification of the active form of a chimeric therapeutic antibody in human serum
    • DOI 10.1021/ac7021234
    • Dubois M, Fenaille F, Clement G et al. Immunopurification and mass spectrometric quantification of the active form of a chimeric therapeutic antibody in human serum. Anal. Chem. 80(5), 1737-1745 (2008). (Pubitemid 351429580)
    • (2008) Analytical Chemistry , vol.80 , Issue.5 , pp. 1737-1745
    • Dubois, M.1    Fenaille, F.2    Clement, G.3    Lechmann, M.4    Tabet, J.-C.5    Ezan, E.6    Becher, F.7
  • 19
    • 70350637466 scopus 로고    scopus 로고
    • Development of different analysis platforms with LC-MS for pharmacokinetic studies of protein drugs
    • Lu Q, Zheng X, Mcintosh T et al. Development of different analysis platforms with LC-MS for pharmacokinetic studies of protein drugs. Anal. Chem. 81(21), 8715-8723 (2009).
    • (2009) Anal. Chem , vol.81 , Issue.21 , pp. 8715-8723
    • Lu, Q.1    Zheng, X.2    McIntosh, T.3
  • 20
    • 84863012569 scopus 로고    scopus 로고
    • General LC-MS/MS method approach to quantify therapeutic monoclonal antibodies using a common whole antibody internal standard with application to preclinical studies
    • Li H, Ortiz R, Tran L et al. General LC-MS/MS method approach to quantify therapeutic monoclonal antibodies using a common whole antibody internal standard with application to preclinical studies. Anal. Chem. 84(3), 1267-1273 (2012).
    • (2012) Anal. Chem , vol.84 , Issue.3 , pp. 1267-1273
    • Li, H.1    Ortiz, R.2    Tran, L.3
  • 21
    • 59149092065 scopus 로고    scopus 로고
    • Mass spectrometry for structural characterization of therapeutic antibodies
    • Zhang Z, Pan H, Chen X. Mass spectrometry for structural characterization of therapeutic antibodies. Mass Spectrom. Rev. 28(1), 147-176 (2009).
    • (2009) Mass Spectrom. Rev , vol.28 , Issue.1 , pp. 147-176
    • Zhang, Z.1    Pan, H.2    Chen, X.3
  • 22
    • 84855740330 scopus 로고    scopus 로고
    • Advances and challenges in analytical characterization of biotechnology products: Mass spectrometry-based approaches to study properties and behavior of protein therapeutics
    • Kaltashov IA, Bobst CE, Abzalimov RR, Wang G, Baykal B, Wang S. Advances and challenges in analytical characterization of biotechnology products: mass spectrometry-based approaches to study properties and behavior of protein therapeutics. Biotechnol. Adv. 30(1), 210-222 (2012).
    • (2012) Biotechnol. Adv , vol.30 , Issue.1 , pp. 210-222
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3    Wang, G.4    Baykal, B.5    Wang, S.6
  • 23
    • 39149138479 scopus 로고    scopus 로고
    • Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid
    • Ryan MH, Petrone D, Nemeth JF, Barnathan E, Bjorck L, Jordan RE. Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid. Mol. Immunol. 45(7), 1837-1846 (2008).
    • (2008) Mol. Immunol , vol.45 , Issue.7 , pp. 1837-1846
    • Ryan, M.H.1    Petrone, D.2    Nemeth, J.F.3    Barnathan, E.4    Bjorck, L.5    Jordan, R.E.6
  • 24
    • 70349762761 scopus 로고    scopus 로고
    • Electrospray ionization quadrupole ion-mobility time-of-flight mass spectrometry as a tool to distinguish the lot-to-lot heterogeneity in N-glycosylation profile of the therapeutic monoclonal antibody trastuzumab
    • Damen CW, Chen W, Chakraborty AB et al. Electrospray ionization quadrupole ion-mobility time-of-flight mass spectrometry as a tool to distinguish the lot-to-lot heterogeneity in N-glycosylation profile of the therapeutic monoclonal antibody trastuzumab. J. Am. Soc. Mass Spectrom. 20(11), 2021-2033 (2009).
    • (2009) J. Am. Soc. Mass Spectrom , vol.20 , Issue.11 , pp. 2021-2033
    • Damen, C.W.1    Chen, W.2    Chakraborty, A.B.3
  • 26
    • 46749112184 scopus 로고    scopus 로고
    • Fragmentation of a recombinant monoclonal antibody at various pH
    • Gaza-Bulseco G, Liu H. Fragmentation of a recombinant monoclonal antibody at various pH. Pharm. Res. 25(8), 1881-1890 (2008).
    • (2008) Pharm. Res , vol.25 , Issue.8 , pp. 1881-1890
    • Gaza-Bulseco, G.1    Liu, H.2
  • 27
    • 64149109989 scopus 로고    scopus 로고
    • Impact of methionine oxidation on the binding of human IgG1 to Fc Rn and Fc gamma receptors
    • Bertolotti-Ciarlet A, Wang W, Lownes R et al. Impact of methionine oxidation on the binding of human IgG1 to Fc Rn and Fc gamma receptors. Mol. Immunol. 46(8-9), 1878-1882 (2009).
    • (2009) Mol. Immunol , vol.46 , Issue.8-9 , pp. 1878-1882
    • Bertolotti-Ciarlet, A.1    Wang, W.2    Lownes, R.3
  • 28
    • 45849089529 scopus 로고    scopus 로고
    • Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G. J
    • Gaza-Bulseco G, Faldu S, Hurkmans K, Chumsae C, Liu H. Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 870(1), 55-62 (2008).
    • (2008) Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.870 , Issue.1 , pp. 55-62
    • Gaza-Bulseco, G.1    Faldu, S.2    Hurkmans, K.3    Chumsae, C.4    Liu, H.5
  • 30
    • 71649111437 scopus 로고    scopus 로고
    • The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies
    • Banks DD, Hambly DM, Scavezze JL, Siska CC, Stackhouse NL, Gadgil HS. The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies. J. Pharm. Sci. 98(12), 4501-4510 (2009).
    • (2009) J. Pharm. Sci , vol.98 , Issue.12 , pp. 4501-4510
    • Banks, D.D.1    Hambly, D.M.2    Scavezze, J.L.3    Siska, C.C.4    Stackhouse, N.L.5    Gadgil, H.S.6
  • 31
    • 84862907501 scopus 로고    scopus 로고
    • Rates and impact of human antibody glycation in vivo
    • Goetze AM, Liu YD, Arroll T, Chu L, Flynn GC. Rates and impact of human antibody glycation in vivo. Glycobiology 22(2), 221-234 (2012).
    • (2012) Glycobiology , vol.22 , Issue.2 , pp. 221-234
    • Goetze, A.M.1    Liu, Y.D.2    Arroll, T.3    Chu, L.4    Flynn, G.C.5
  • 32
    • 33645697563 scopus 로고    scopus 로고
    • Formation of pyroglutamic acid from N-terminal glutamic acid in immunoglobulin gamma antibodies
    • Chelius D, Jing K, Lueras A et al. Formation of pyroglutamic acid from N-terminal glutamic acid in immunoglobulin gamma antibodies. Anal. Chem. 78(7), 2370-2376 (2006).
    • (2006) Anal. Chem , vol.78 , Issue.7 , pp. 2370-2376
    • Chelius, D.1    Jing, K.2    Lueras, A.3
  • 33
    • 60849102492 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods
    • Vlasak J, Ionescu R. Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods. Curr. Pharm. Biotechnol. 9(6), 468-481 (2008).
    • (2008) Curr. Pharm. Biotechnol , vol.9 , Issue.6 , pp. 468-481
    • Vlasak, J.1    Ionescu, R.2
  • 34
    • 77951498805 scopus 로고    scopus 로고
    • Protein aggregation-pathways and influencing factors
    • Wang W, Nema S, Teagarden D. Protein aggregation-pathways and influencing factors. Int. J. Pharm. 390(2), 89-99 (2010).
    • (2010) Int. J. Pharm , vol.390 , Issue.2 , pp. 89-99
    • Wang, W.1    Nema, S.2    Teagarden, D.3
  • 35
    • 33847059215 scopus 로고    scopus 로고
    • Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies
    • Ejima D, Tsumoto K, Fukada H et al. Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies. Proteins 66(4), 954-962 (2007).
    • (2007) Proteins , vol.66 , Issue.4 , pp. 954-962
    • Ejima, D.1    Tsumoto, K.2    Fukada, H.3
  • 36
    • 78049249356 scopus 로고    scopus 로고
    • Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies
    • Sahin E, Grillo AO, Perkins MD, Roberts CJ. Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies. J. Pharm. Sci. 99(12), 4830-4848 (2010).
    • (2010) J. Pharm. Sci , vol.99 , Issue.12 , pp. 4830-4848
    • Sahin, E.1    Grillo, A.O.2    Perkins, M.D.3    Roberts, C.J.4
  • 37
    • 84859313113 scopus 로고    scopus 로고
    • Effect of pH and light on aggregation and conformation of an IgG1 mAb
    • Mason BD, Schoneich C, Kerwin BA. Effect of pH and light on aggregation and conformation of an IgG1 mAb. Mol. Pharm. 9(4), 774-790 (2012).
    • (2012) Mol. Pharm , vol.9 , Issue.4 , pp. 774-790
    • Mason, B.D.1    Schoneich, C.2    Kerwin, B.A.3
  • 38
    • 79955638418 scopus 로고    scopus 로고
    • Strategies for the assessment of protein aggregates in pharmaceutical biotech product development
    • Den Engelsman J, Garidel P, Smulders R et al. Strategies for the assessment of protein aggregates in pharmaceutical biotech product development. Pharm. Res. 28(4), 920-933 (2011).
    • (2011) Pharm. Res , vol.28 , Issue.4 , pp. 920-933
    • Den Engelsman, J.1    Garidel, P.2    Smulders, R.3
  • 39
    • 84864452495 scopus 로고    scopus 로고
    • Structure and function of purified monoclonal antibody dimers induced by different stress conditions
    • Paul R, Graff-Meyer A, Stahlberg H et al. Structure and function of purified monoclonal antibody dimers induced by different stress conditions. Pharm. Res. 29(8), 2047-2059 (2012).
    • (2012) Pharm. Res , vol.29 , Issue.8 , pp. 2047-2059
    • Paul, R.1    Graff-Meyer, A.2    Stahlberg, H.3
  • 40
    • 79960135244 scopus 로고    scopus 로고
    • Chemical modifications in therapeutic protein aggregates generated under different stress conditions
    • Luo Q, Joubert MK, Stevenson R, Ketchem Rr, Narhi LO, Wypych J. Chemical modifications in therapeutic protein aggregates generated under different stress conditions. J. Biol. Chem. 286(28), 25134-25144 (2011).
    • (2011) J. Biol. Chem , vol.286 , Issue.28 , pp. 25134-25144
    • Luo, Q.1    Joubert, M.K.2    Stevenson, R.3    Rr, K.4    Narhi, L.O.5    Wypych, J.6
  • 42
    • 77955412238 scopus 로고    scopus 로고
    • Post-translational modifications differentially affect IgG1 conformation and receptor binding
    • Houde D, Peng Y, Berkowitz SA, Engen JR. Post-translational modifications differentially affect IgG1 conformation and receptor binding. Mol. Cell. Proteomics 9(8), 1716-1728 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.8 , pp. 1716-1728
    • Houde, D.1    Peng, Y.2    Berkowitz, S.A.3    Engen, J.R.4
  • 44
    • 30744439811 scopus 로고    scopus 로고
    • Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298
    • DOI 10.1016/j.ijpharm.2005.10.024, PII S0378517305007076
    • Zheng JY, Janis LJ. Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298. Int. J. Pharm. 308(1-2), 46-51 (2006). (Pubitemid 43097234)
    • (2006) International Journal of Pharmaceutics , vol.308 , Issue.1-2 , pp. 46-51
    • Zheng, J.Y.1    Janis, L.J.2
  • 45
    • 67650482859 scopus 로고    scopus 로고
    • Identification and characterization of asparagine deamidation in the light chain CDR1 of a humanized IgG1 antibody
    • Vlasak J, Bussat MC, Wang S et al. Identification and characterization of asparagine deamidation in the light chain CDR1 of a humanized IgG1 antibody. Anal. Biochem. 392(2), 145-154 (2009).
    • (2009) Anal. Biochem , vol.392 , Issue.2 , pp. 145-154
    • Vlasak, J.1    Bussat, M.C.2    Wang, S.3
  • 46
    • 33846967443 scopus 로고    scopus 로고
    • Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies
    • Wakankar AA, Borchardt RT, Eigenbrot C et al. Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies. Biochemistry 46(6), 1534-1544 (2007).
    • (2007) Biochemistry , vol.46 , Issue.6 , pp. 1534-1544
    • Wakankar, A.A.1    Borchardt, R.T.2    Eigenbrot, C.3
  • 49
    • 77956355090 scopus 로고    scopus 로고
    • Increased aggregation propensity of IgG2 subclass over IgG1: Role of conformational changes and covalent character in isolated aggregates
    • Franey H, Brych SR, Kolvenbach CG, Rajan RS. Increased aggregation propensity of IgG2 subclass over IgG1: role of conformational changes and covalent character in isolated aggregates. Protein Sci. 19(9), 1601-1615 (2010).
    • (2010) Protein Sci , vol.19 , Issue.9 , pp. 1601-1615
    • Franey, H.1    Brych, S.R.2    Kolvenbach, C.G.3    Rajan, R.S.4
  • 50
    • 84863045993 scopus 로고    scopus 로고
    • Disulfide bond structures of IgG molecules: Structural variations, chemical modifications and possible impacts to stability and biological function
    • Liu H, May K. Disulfide bond structures of IgG molecules: structural variations, chemical modifications and possible impacts to stability and biological function. MAbs 4(1), 17-23 (2012).
    • (2012) MAbs , vol.4 , Issue.1 , pp. 17-23
    • Liu, H.1    May, K.2
  • 52
    • 77958549515 scopus 로고    scopus 로고
    • Rapid comparison of a candidate biosimilar to an innovator monoclonal antibody with advanced liquid chromatography and mass spectrometry technologies
    • Xie H, Chakraborty A, Ahn J et al. Rapid comparison of a candidate biosimilar to an innovator monoclonal antibody with advanced liquid chromatography and mass spectrometry technologies. MAbs 2(4), (2010).
    • (2010) MAbs , vol.2 , Issue.4
    • Xie, H.1    Chakraborty, A.2    Ahn, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.