메뉴 건너뛰기




Volumn 69, Issue , 2012, Pages 185-195

Analytical aspects of biosimilarity issues of protein drugs

Author keywords

Biosimilar; Comparability; Immunogenicity; Protein analysis; Protein heterogeneity

Indexed keywords

BIOSIMILAR AGENT; DRUG ADDITIVE; GENETROPIN; HUMAN GROWTH HORMONE; RECOMBINANT ERYTHROPOIETIN; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; SILAPRO; UNCLASSIFIED DRUG;

EID: 84865077796     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2012.04.037     Document Type: Review
Times cited : (43)

References (121)
  • 5
    • 79952744875 scopus 로고    scopus 로고
    • Worldwide experience with biosimilar development
    • McCamish M., Woollett G. Worldwide experience with biosimilar development. mAbs 2011, 3:209-217.
    • (2011) mAbs , vol.3 , pp. 209-217
    • McCamish, M.1    Woollett, G.2
  • 6
    • 84865087276 scopus 로고    scopus 로고
    • CHMP, European Medicines Agency, 2011, Guideline on Similar Biological Medicinal Products Containing Biotechnology-Derived Proteins as Active Substance: Quality Issues, EMEA/CHMP/BWP/49348/2005, 30th September
    • CHMP, European Medicines Agency, 2011, Guideline on Similar Biological Medicinal Products Containing Biotechnology-Derived Proteins as Active Substance: Quality Issues, EMEA/CHMP/BWP/49348/2005, 30th September 2011.
    • (2011)
  • 7
    • 0029812368 scopus 로고    scopus 로고
    • Identification and characterization of glycopeptides in tryptic maps by high-pH anion-exchange chromatography
    • Academic Press, W.S.H. Barry, L. Karger (Eds.)
    • Townsend R.R., Basa L.J., Spellman M.W. Identification and characterization of glycopeptides in tryptic maps by high-pH anion-exchange chromatography. Methods in Enzymology 1996, 135-147. Academic Press. W.S.H. Barry, L. Karger (Eds.).
    • (1996) Methods in Enzymology , pp. 135-147
    • Townsend, R.R.1    Basa, L.J.2    Spellman, M.W.3
  • 8
    • 30544443201 scopus 로고    scopus 로고
    • Identification of phosphorylation sites using microimmobilized metal affinity chromatography
    • Academic Press, A.L. Burlingame (Ed.)
    • Corthals G.L., Aebersold R., Goodlett D.R. Identification of phosphorylation sites using microimmobilized metal affinity chromatography. Methods in Enzymology 2005, 66-81. Academic Press. A.L. Burlingame (Ed.).
    • (2005) Methods in Enzymology , pp. 66-81
    • Corthals, G.L.1    Aebersold, R.2    Goodlett, D.R.3
  • 9
    • 0025672798 scopus 로고
    • Strategies for locating disulfide bonds in proteins
    • Academic Press, A.M. James (Ed.)
    • Smith D.L., Zhou Z. Strategies for locating disulfide bonds in proteins. Methods in Enzymology 1990, 374-389. Academic Press. A.M. James (Ed.).
    • (1990) Methods in Enzymology , pp. 374-389
    • Smith, D.L.1    Zhou, Z.2
  • 10
    • 30544452187 scopus 로고    scopus 로고
    • Mapping posttranslational modifications of proteins by MS-based selective detection: application to phosphoproteomics
    • Academic Press, A.L. Burlingame (Ed.)
    • Carr S.A., Annan R.S., Huddleston M.J. Mapping posttranslational modifications of proteins by MS-based selective detection: application to phosphoproteomics. Methods in Enzymology 2005, 82-115. Academic Press. A.L. Burlingame (Ed.).
    • (2005) Methods in Enzymology , pp. 82-115
    • Carr, S.A.1    Annan, R.S.2    Huddleston, M.J.3
  • 11
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg P.J. Disulfide bonds as switches for protein function. Trends Biochem. Sci. 2003, 28:210-214.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 12
    • 79959212598 scopus 로고    scopus 로고
    • Interfacial immobilization of monoclonal antibody and detection of human prostate-specific antigen
    • Zhao X., Pan F., Cowsill B., Lu J.R., Garcia-Gancedo L., Flewitt A.J., Ashley G.M., Luo J. Interfacial immobilization of monoclonal antibody and detection of human prostate-specific antigen. Langmuir 2011, 27:7654-7662.
    • (2011) Langmuir , vol.27 , pp. 7654-7662
    • Zhao, X.1    Pan, F.2    Cowsill, B.3    Lu, J.R.4    Garcia-Gancedo, L.5    Flewitt, A.J.6    Ashley, G.M.7    Luo, J.8
  • 14
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris P.I., Severcan F. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. J. Mol. Catal. B: Enzym. 1999, 7:207-221.
    • (1999) J. Mol. Catal. B: Enzym. , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 16
    • 71549136813 scopus 로고    scopus 로고
    • Chapter 40 Identification and quantification of protein posttranslational modifications
    • Academic Press, R.B. Richard, P.D. Murray (Eds.)
    • Farley A.R., Link A.J. Chapter 40 Identification and quantification of protein posttranslational modifications. Methods in Enzymology 2009, 725-763. Academic Press. R.B. Richard, P.D. Murray (Eds.).
    • (2009) Methods in Enzymology , pp. 725-763
    • Farley, A.R.1    Link, A.J.2
  • 17
    • 84865095263 scopus 로고    scopus 로고
    • CBER, CDER, U.S. Food and Drug Administration (FDA), 1996, Demonstration of Comparability of Human Biological Products, Including Therapeutic Biotechnology-derived Products, April
    • CBER, CDER, U.S. Food and Drug Administration (FDA), 1996, Demonstration of Comparability of Human Biological Products, Including Therapeutic Biotechnology-derived Products, April 1996.
    • (1996)
  • 18
    • 84865095262 scopus 로고    scopus 로고
    • CHMP, European Medicines Agency, London, Concept Paper on the Development of a Guideline on Similar Biological Medicinal Products Containing Monoclonal Antibodies.
    • CHMP, European Medicines Agency, London, 2009, Concept Paper on the Development of a Guideline on Similar Biological Medicinal Products Containing Monoclonal Antibodies.
    • (2009)
  • 19
    • 77955842549 scopus 로고    scopus 로고
    • Modulation of quaternary structure of S100 proteins by calcium ions
    • Streicher W.W., Lopez M.M., Makhatadze G.I. Modulation of quaternary structure of S100 proteins by calcium ions. Biophys. Chem. 2010, 151:181-186.
    • (2010) Biophys. Chem. , vol.151 , pp. 181-186
    • Streicher, W.W.1    Lopez, M.M.2    Makhatadze, G.I.3
  • 22
    • 0024373677 scopus 로고
    • Two-dimensional NMR and protein structure
    • Bax A. Two-dimensional NMR and protein structure. Annu. Rev. Biochem. 1989, 58:223-256.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 223-256
    • Bax, A.1
  • 24
    • 0027375364 scopus 로고
    • Peptide mass maps: a highly informative approach to protein identification
    • Yates J.R., Speicher S., Griffin P.R., Hunkapiller T. Peptide mass maps: a highly informative approach to protein identification. Anal. Biochem. 1993, 214:397-408.
    • (1993) Anal. Biochem. , vol.214 , pp. 397-408
    • Yates, J.R.1    Speicher, S.2    Griffin, P.R.3    Hunkapiller, T.4
  • 25
    • 4444335470 scopus 로고    scopus 로고
    • The abc's (and xyz's) of peptide sequencing
    • Steen H., Mann M. The abc's (and xyz's) of peptide sequencing. Nat. Rev. Mol. Cell Biol. 2004, 5:699-711.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 26
    • 0001433809 scopus 로고
    • Method for determination of the amino acid sequence in peptides
    • Edman P. Method for determination of the amino acid sequence in peptides. Acta Chem. Scand. 1950, 4:283-293.
    • (1950) Acta Chem. Scand. , vol.4 , pp. 283-293
    • Edman, P.1
  • 27
    • 84865100056 scopus 로고    scopus 로고
    • Current status of protein quantification technologies
    • Aschermann K., Lutter P., Wattenberg A. Current status of protein quantification technologies. Bioprocess Int. 2008, 6:44-53.
    • (2008) Bioprocess Int. , vol.6 , pp. 44-53
    • Aschermann, K.1    Lutter, P.2    Wattenberg, A.3
  • 28
    • 33845747314 scopus 로고    scopus 로고
    • Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain
    • Feige M.J., Hagn F., Esser J., Kessler H., Buchner J. Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain. J. Mol. Biol. 2007, 365:1232-1244.
    • (2007) J. Mol. Biol. , vol.365 , pp. 1232-1244
    • Feige, M.J.1    Hagn, F.2    Esser, J.3    Kessler, H.4    Buchner, J.5
  • 31
    • 77955606264 scopus 로고    scopus 로고
    • Resolving disulfide structural isoforms of IgG2 monoclonal antibodies by ion mobility mass spectrometry
    • Bagal D., Valliere-Douglass J.F., Balland A., Schnier P.D. Resolving disulfide structural isoforms of IgG2 monoclonal antibodies by ion mobility mass spectrometry. Anal. Chem. 2010, 82:6751-6755.
    • (2010) Anal. Chem. , vol.82 , pp. 6751-6755
    • Bagal, D.1    Valliere-Douglass, J.F.2    Balland, A.3    Schnier, P.D.4
  • 32
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe A., Sutter M., Jiskoot W. Extrinsic fluorescent dyes as tools for protein characterization. Pharm. Res. 2008, 25:1487-1499.
    • (2008) Pharm. Res. , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 34
    • 40549086568 scopus 로고    scopus 로고
    • Automated technologies and novel techniques to accelerate protein crystallography for structural genomics
    • Manjasetty B.A., Turnbull A.P., Panjikar S., Büssow K., Chance M.R. Automated technologies and novel techniques to accelerate protein crystallography for structural genomics. Proteomics 2008, 8:612-625.
    • (2008) Proteomics , vol.8 , pp. 612-625
    • Manjasetty, B.A.1    Turnbull, A.P.2    Panjikar, S.3    Büssow, K.4    Chance, M.R.5
  • 36
    • 84865095686 scopus 로고    scopus 로고
    • CBER, CDER, U.S. Food and Drug Administration (FDA), Q6B Specifications: Test Procedures and Acceptance Criteria for Biotechnological/Biological Products.
    • CBER, CDER, U.S. Food and Drug Administration (FDA), 1999, Q6B Specifications: Test Procedures and Acceptance Criteria for Biotechnological/Biological Products.
    • (1999)
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry O.H., Farr N.J., Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193:265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Farr, N.J.2    Randall, R.J.3
  • 41
    • 69449095403 scopus 로고    scopus 로고
    • Biosimilar therapeutics-what do we need to consider?
    • Schellekens H. Biosimilar therapeutics-what do we need to consider?. Clin. Kidney J. 2008, 2:27-36.
    • (2008) Clin. Kidney J. , vol.2 , pp. 27-36
    • Schellekens, H.1
  • 42
    • 77954861342 scopus 로고    scopus 로고
    • Correlation of liquid chromatographic and biological assay for potency assessment of filgrastim and related impurities
    • Skrlin A., Krnic E.K., Gosak D., Prester B., Mrsa V., Vuletic M., Runac D. Correlation of liquid chromatographic and biological assay for potency assessment of filgrastim and related impurities. J. Pharm. Biomed. Anal. 2010, 53:262-268.
    • (2010) J. Pharm. Biomed. Anal. , vol.53 , pp. 262-268
    • Skrlin, A.1    Krnic, E.K.2    Gosak, D.3    Prester, B.4    Mrsa, V.5    Vuletic, M.6    Runac, D.7
  • 43
  • 44
    • 21444442363 scopus 로고    scopus 로고
    • Biosimilar epoetins: an analysis based on recently implemented European medicines evaluation agency guidelines on comparability of biopharmaceutical proteins
    • Combe C., Tredree R.L., Schellekens H. Biosimilar epoetins: an analysis based on recently implemented European medicines evaluation agency guidelines on comparability of biopharmaceutical proteins. Pharmacotherapy 2005, 25:954-962.
    • (2005) Pharmacotherapy , vol.25 , pp. 954-962
    • Combe, C.1    Tredree, R.L.2    Schellekens, H.3
  • 45
  • 46
    • 70049109465 scopus 로고    scopus 로고
    • Binocrit: assessment of quality, safety and efficacy of biopharmaceuticals
    • Brockmeyer C., Seidl A. Binocrit: assessment of quality, safety and efficacy of biopharmaceuticals. Eur. J. Hosp. Pharm. Practice 2009, 15:34-40.
    • (2009) Eur. J. Hosp. Pharm. Practice , vol.15 , pp. 34-40
    • Brockmeyer, C.1    Seidl, A.2
  • 47
    • 19044374719 scopus 로고    scopus 로고
    • Biosimilar epoetins: how similar are they?
    • Schellekens H. Biosimilar epoetins: how similar are they?. Eur. J. Hosp. Pharm. 2004, 3:43-47.
    • (2004) Eur. J. Hosp. Pharm. , vol.3 , pp. 43-47
    • Schellekens, H.1
  • 49
    • 78049515273 scopus 로고    scopus 로고
    • Physicochemical and biologic comparability of a biosimilar granulocyte colony-stimulating factor with its reference product
    • Sörgel F., Lerch H., Lauber T. Physicochemical and biologic comparability of a biosimilar granulocyte colony-stimulating factor with its reference product. BioDrugs 2010, 24:347-357.
    • (2010) BioDrugs , vol.24 , pp. 347-357
    • Sörgel, F.1    Lerch, H.2    Lauber, T.3
  • 50
    • 0035424309 scopus 로고    scopus 로고
    • Post-translational protein modifications in antigen recognition and autoimmunity
    • Doyle H.A., Mamula M.J. Post-translational protein modifications in antigen recognition and autoimmunity. Trends Immunol. 2001, 22:443-449.
    • (2001) Trends Immunol. , vol.22 , pp. 443-449
    • Doyle, H.A.1    Mamula, M.J.2
  • 52
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold J.N., Wormald M.R., Sim R.B., Rudd P.M., Dwek R.A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25:21-50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 53
    • 68149141340 scopus 로고    scopus 로고
    • The challenges of immunogenicity in developing biosimilar products
    • Wadhwa M., Thorpe R. The challenges of immunogenicity in developing biosimilar products. IDrugs 2009, 12:440-444.
    • (2009) IDrugs , vol.12 , pp. 440-444
    • Wadhwa, M.1    Thorpe, R.2
  • 54
    • 0035158301 scopus 로고    scopus 로고
    • Human immune response to recombinant human proteins
    • Porter S. Human immune response to recombinant human proteins. J. Pharm. Sci. 2001, 90:1-11.
    • (2001) J. Pharm. Sci. , vol.90 , pp. 1-11
    • Porter, S.1
  • 56
    • 0033763507 scopus 로고    scopus 로고
    • Immunogenicity of interferon-beta in multiple sclerosis patients: influence of preparation, dosage, dose frequency, and route of administration. Danish Multiple Sclerosis Study Group
    • Ross C., Clemmesen K.M., Svenson M., Sörensen P.S., Koch-Henriksen N., Skovgaard G.L., Bendtzen K. Immunogenicity of interferon-beta in multiple sclerosis patients: influence of preparation, dosage, dose frequency, and route of administration. Danish Multiple Sclerosis Study Group. Ann. Neurol. 2000, 48:706-712.
    • (2000) Ann. Neurol. , vol.48 , pp. 706-712
    • Ross, C.1    Clemmesen, K.M.2    Svenson, M.3    Sörensen, P.S.4    Koch-Henriksen, N.5    Skovgaard, G.L.6    Bendtzen, K.7
  • 57
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenicity relationships of therapeutic proteins
    • Hermeling S., Crommelin D., Schellekens H., Jiskoot W. Structure-immunogenicity relationships of therapeutic proteins. Pharm. Res. 2004, 21:897-903.
    • (2004) Pharm. Res. , vol.21 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.2    Schellekens, H.3    Jiskoot, W.4
  • 58
    • 77957336916 scopus 로고    scopus 로고
    • The immunogenicity of therapeutic proteins
    • Schellekens H. The immunogenicity of therapeutic proteins. Discov. Med. 2010, 9:560-564.
    • (2010) Discov. Med. , vol.9 , pp. 560-564
    • Schellekens, H.1
  • 59
    • 79551582036 scopus 로고    scopus 로고
    • Solution ELISA as a platform of choice for development of robust, drug tolerant immunogenicity assays in support of drug development
    • Mikulskis A., Yeung D., Subramanyam M., Amaravadi L., Solution ELISA as a platform of choice for development of robust, drug tolerant immunogenicity assays in support of drug development. J. Immunol. Methods 2011, 365:38-49.
    • (2011) J. Immunol. Methods , vol.365 , pp. 38-49
    • Mikulskis, A.1    Yeung, D.2    Subramanyam, M.3    Amaravadi, L.4
  • 60
    • 77956873702 scopus 로고    scopus 로고
    • Pharmacokinetic, pharmacodynamic and immunogenicity comparability assessment strategies for monoclonal antibodies
    • Putnam W.S., Prabhu S., Zheng Y., Subramanyam M., Wang Y.-M.C. Pharmacokinetic, pharmacodynamic and immunogenicity comparability assessment strategies for monoclonal antibodies. Trends Biotechnol. 2010, 28:509-516.
    • (2010) Trends Biotechnol. , vol.28 , pp. 509-516
    • Putnam, W.S.1    Prabhu, S.2    Zheng, Y.3    Subramanyam, M.4    Wang, Y.-M.C.5
  • 63
    • 54849437047 scopus 로고    scopus 로고
    • Prediction of immunogenicity: in silico paradigms, ex vivo and in vivo correlates
    • De Groot A.S., McMurry J., Moise L. Prediction of immunogenicity: in silico paradigms, ex vivo and in vivo correlates. Curr. Opin. Pharmacol. 2008, 8:620-626.
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 620-626
    • De Groot, A.S.1    McMurry, J.2    Moise, L.3
  • 64
    • 77953658260 scopus 로고    scopus 로고
    • The immunogenicity of humanized and fully human antibodies: residual immunogenicity resides in the CDR regions
    • Harding F.A., Stickler M.M., Razo J., DuBridge R. The immunogenicity of humanized and fully human antibodies: residual immunogenicity resides in the CDR regions. mAbs 2010, 2:256-265.
    • (2010) mAbs , vol.2 , pp. 256-265
    • Harding, F.A.1    Stickler, M.M.2    Razo, J.3    DuBridge, R.4
  • 66
    • 75149152376 scopus 로고    scopus 로고
    • Prediction of immunogenicity of therapeutic proteins: validity of computational tools
    • Bryson C.J., Jones T.D., Baker M.P. Prediction of immunogenicity of therapeutic proteins: validity of computational tools. BioDrugs 2010, 24:1-8.
    • (2010) BioDrugs , vol.24 , pp. 1-8
    • Bryson, C.J.1    Jones, T.D.2    Baker, M.P.3
  • 67
    • 80054743161 scopus 로고    scopus 로고
    • Oxidized and aggregated recombinant human interferon beta is immunogenic in human interferon beta transgenic mice
    • Beers M.M.C., Sauerborn M., Gilli F., Brinks V., Schellekens H., Jiskoot W. Oxidized and aggregated recombinant human interferon beta is immunogenic in human interferon beta transgenic mice. Pharm. Res. 2011, 28:2393-2402.
    • (2011) Pharm. Res. , vol.28 , pp. 2393-2402
    • Beers, M.M.C.1    Sauerborn, M.2    Gilli, F.3    Brinks, V.4    Schellekens, H.5    Jiskoot, W.6
  • 69
    • 70350457586 scopus 로고    scopus 로고
    • In silico methods for predicting T-cell epitopes: Dr Jekyll or Mr Hyde?
    • Gowthaman U., Agrewala J.N. In silico methods for predicting T-cell epitopes: Dr Jekyll or Mr Hyde?. Expert Rev. Proteomics 2009, 6:527-537.
    • (2009) Expert Rev. Proteomics , vol.6 , pp. 527-537
    • Gowthaman, U.1    Agrewala, J.N.2
  • 70
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: an immunologic perspective
    • Rosenberg A.S. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006, 8:E501-E507.
    • (2006) AAPS J. , vol.8
    • Rosenberg, A.S.1
  • 74
    • 0042009405 scopus 로고    scopus 로고
    • Relationship between biopharmaceutical immunogenicity of epoetin alfa and pure red cell aplasia
    • Schellekens H. Relationship between biopharmaceutical immunogenicity of epoetin alfa and pure red cell aplasia. Curr. Med. Res. Opin. 2003, 19:433-434.
    • (2003) Curr. Med. Res. Opin. , vol.19 , pp. 433-434
    • Schellekens, H.1
  • 75
    • 34547464547 scopus 로고    scopus 로고
    • Amgen, Thousand Oaks, CA, 6th January 2012.
    • Epogen. Full Prescribing Information 2012, Amgen, Thousand Oaks, CA, 6th January 2012.
    • (2012) Epogen. Full Prescribing Information
  • 77
    • 46149124807 scopus 로고    scopus 로고
    • How to predict and prevent the immunogenicity of therapeutic proteins
    • Elsevier, M.R. El-Gewely (Ed.)
    • Schellekens H. How to predict and prevent the immunogenicity of therapeutic proteins. Biotechnol. Ann. Rev. 2008, 191-202. Elsevier. M.R. El-Gewely (Ed.).
    • (2008) Biotechnol. Ann. Rev. , pp. 191-202
    • Schellekens, H.1
  • 78
    • 19044381985 scopus 로고    scopus 로고
    • Antibody-mediated pure red cell aplasia (PRCA): epidemiology, immunogenicity and risks
    • Macdougall I.C. Antibody-mediated pure red cell aplasia (PRCA): epidemiology, immunogenicity and risks. Nephrol. Dial. Transplant. 2005, 20:iv9-iv15.
    • (2005) Nephrol. Dial. Transplant. , vol.20
    • Macdougall, I.C.1
  • 79
    • 84872829995 scopus 로고    scopus 로고
    • MHRA, Eprex® (Epoetin Alfa) and pure red cell aplasia-contraindication of subcutaneous administration to patients with chronic renal disease.
    • A. Breckenridge, MHRA, 2010, Eprex® (Epoetin Alfa) and pure red cell aplasia-contraindication of subcutaneous administration to patients with chronic renal disease.
    • (2010)
    • Breckenridge, A.1
  • 80
    • 84865062932 scopus 로고    scopus 로고
    • CHMP, European Medicines Agency, London, Questions and Ansvers on Recommendation for Refusal of Marketing Application for Alferon, EMEA/190896/2006.
    • CHMP, European Medicines Agency, London, 2006, Questions and Ansvers on Recommendation for Refusal of Marketing Application for Alferon, EMEA/190896/2006.
    • (2006)
  • 81
    • 70350776252 scopus 로고    scopus 로고
    • Therapeutic equivalence, long-term efficacy and safety of HX575 in the treatment of anemia in chronic renal failure patients receiving hemodialysis
    • Haag-Weber M., Vetter A., Thyroff-Friesinger U., Group I.-S. Therapeutic equivalence, long-term efficacy and safety of HX575 in the treatment of anemia in chronic renal failure patients receiving hemodialysis. Clin. Nephrol. 2009, 72:380-390.
    • (2009) Clin. Nephrol. , vol.72 , pp. 380-390
    • Haag-Weber, M.1    Vetter, A.2    Thyroff-Friesinger, U.3    Group, I.-S.4
  • 82
    • 80053562430 scopus 로고    scopus 로고
    • Clinical programs in the development of similar biotherapeutic products: rationale and general principles
    • Berghout A. Clinical programs in the development of similar biotherapeutic products: rationale and general principles. Biologicals 2011, 39:293-296.
    • (2011) Biologicals , vol.39 , pp. 293-296
    • Berghout, A.1
  • 83
    • 84872828537 scopus 로고    scopus 로고
    • EMEA, Omnitrope: scientific discussion
    • EMEA, 2006, Omnitrope: scientific discussion, http://www.ema.europa.eu/docs/en_GB/document_library/EPAR_-_Scientific_Discussion/human/000607/WC500043692.pdf.
    • (2006)
  • 84
    • 34249908675 scopus 로고    scopus 로고
    • Amgen, 6th January 2012
    • Neupogen. Full prescribing information 2009, Amgen, 6th January 2012, http://pi.amgen.com/united_states/neupogen/neupogen_pi_hcp_english.pdf.
    • (2009) Neupogen. Full prescribing information
  • 87
    • 84865062933 scopus 로고    scopus 로고
    • CDER, CBER, U.S. Food and Drug Administration (FDA), Rockville, MD, USA, 2012, Biosimilars: Questions and Ansvers Regarding Implementation of the Biologics Price Competition Innovation Act of
    • CDER, CBER, U.S. Food and Drug Administration (FDA), Rockville, MD, USA, 2012, Biosimilars: Questions and Ansvers Regarding Implementation of the Biologics Price Competition Innovation Act of 2009, pp. 15.
    • (2009) , pp. 15
  • 88
    • 81155161875 scopus 로고    scopus 로고
    • Quantification of human growth hormone by amino acid composition analysis using isotope dilution liquid-chromatography tandem mass spectrometry
    • Jeong J.-S., Lim H.-M., Kim S.-K., Ku H.-K., Oh K.-H., Park S.-R. Quantification of human growth hormone by amino acid composition analysis using isotope dilution liquid-chromatography tandem mass spectrometry. J. Chromatogr. A 2011, 1218:6596-6602.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 6596-6602
    • Jeong, J.-S.1    Lim, H.-M.2    Kim, S.-K.3    Ku, H.-K.4    Oh, K.-H.5    Park, S.-R.6
  • 89
    • 0003291213 scopus 로고    scopus 로고
    • One-dimensional SDS gel electrophoresis of proteins
    • John Wiley & Sons, Inc.
    • Gallagher S.R. One-dimensional SDS gel electrophoresis of proteins. Current Protocols in Protein Science 2001, John Wiley & Sons, Inc.
    • (2001) Current Protocols in Protein Science
    • Gallagher, S.R.1
  • 91
    • 71549152820 scopus 로고    scopus 로고
    • Chapter 8 quantitation of protein
    • Academic Press, R.B. Richard, P.D. Murray (Eds.)
    • Noble J.E., Bailey M.J.A. Chapter 8 quantitation of protein. Methods in Enzymology 2009, 73-95. Academic Press. R.B. Richard, P.D. Murray (Eds.).
    • (2009) Methods in Enzymology , pp. 73-95
    • Noble, J.E.1    Bailey, M.J.A.2
  • 92
    • 49549086897 scopus 로고    scopus 로고
    • Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches
    • Konermann L., Tong X., Pan Y. Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches. J. Mass Spectrometry 2008, 3:1021-1036.
    • (2008) J. Mass Spectrometry , vol.3 , pp. 1021-1036
    • Konermann, L.1    Tong, X.2    Pan, Y.3
  • 94
    • 84155170823 scopus 로고    scopus 로고
    • Protein separation by capillary gel electrophoresis: a review
    • Zhu Z., Lu J.J., Liu S. Protein separation by capillary gel electrophoresis: a review. Anal. Chim. Acta 2012, 709:21-31.
    • (2012) Anal. Chim. Acta , vol.709 , pp. 21-31
    • Zhu, Z.1    Lu, J.J.2    Liu, S.3
  • 96
    • 80054806761 scopus 로고    scopus 로고
    • Conventional isoelectric focusing in gel slabs and capillaries and immobilized pH gradients
    • John Wiley & Sons, Inc.
    • Righetti P.G., Fasoli E., Righetti S.C. Conventional isoelectric focusing in gel slabs and capillaries and immobilized pH gradients. Protein Purification 2011, John Wiley & Sons, Inc., pp. 379-409.
    • (2011) Protein Purification , pp. 379-409
    • Righetti, P.G.1    Fasoli, E.2    Righetti, S.C.3
  • 99
    • 80054828907 scopus 로고    scopus 로고
    • Capillary electrophoretic separations
    • Thormann W. Capillary electrophoretic separations. Methods Biochem. Anal. 2011, 54:451-485.
    • (2011) Methods Biochem. Anal. , vol.54 , pp. 451-485
    • Thormann, W.1
  • 101
    • 84855544582 scopus 로고    scopus 로고
    • Strong cation exchange chromatography in analysis of posttranslational modifications: innovations and perspectives
    • Edelmann M.J. Strong cation exchange chromatography in analysis of posttranslational modifications: innovations and perspectives. J. Biomed. Biotechnol. 2011, 2011.
    • (2011) J. Biomed. Biotechnol. , vol.2011
    • Edelmann, M.J.1
  • 102
    • 0029686509 scopus 로고    scopus 로고
    • Size-exclusion chromatography
    • Cutler P. Size-exclusion chromatography. Methods Mol. Biol. 1996, 59:255-267.
    • (1996) Methods Mol. Biol. , vol.59 , pp. 255-267
    • Cutler, P.1
  • 103
    • 0025173758 scopus 로고
    • Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds
    • Alpert A.J. Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds. J. Chromatogr. A 1990, 499:177-196.
    • (1990) J. Chromatogr. A , vol.499 , pp. 177-196
    • Alpert, A.J.1
  • 104
    • 84856216972 scopus 로고    scopus 로고
    • Hydrophilic interaction liquid chromatography (HILIC)-a powerful separation technique
    • Buszewski B., Noga S. Hydrophilic interaction liquid chromatography (HILIC)-a powerful separation technique. Anal. Bioanalyt. Chem. 2012, 402:231-247.
    • (2012) Anal. Bioanalyt. Chem. , vol.402 , pp. 231-247
    • Buszewski, B.1    Noga, S.2
  • 105
    • 0021772653 scopus 로고
    • Comparison of hydrophobic-interaction and reversed-phase chromatography of proteins
    • Fausnaugh J.L., Kennedy L.A., Regnier F.E. Comparison of hydrophobic-interaction and reversed-phase chromatography of proteins. J. Chromatogr. A 1984, 317:141-155.
    • (1984) J. Chromatogr. A , vol.317 , pp. 141-155
    • Fausnaugh, J.L.1    Kennedy, L.A.2    Regnier, F.E.3
  • 106
    • 46249099122 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations. II. Hydrophobic interaction
    • Kramarczyk J.F., Kelley B.D., Coffman J.L. High-throughput screening of chromatographic separations. II. Hydrophobic interaction. Biotechnol. Bioengin. 2008, 100:707-720.
    • (2008) Biotechnol. Bioengin. , vol.100 , pp. 707-720
    • Kramarczyk, J.F.1    Kelley, B.D.2    Coffman, J.L.3
  • 107
    • 0022980290 scopus 로고
    • Solution structure of human growth hormone releasing factor: combined use of circular dichroism and nuclear magnetic resonance spectroscopy
    • Clore G.M., Martin S.R., Gronenborn A.M. Solution structure of human growth hormone releasing factor: combined use of circular dichroism and nuclear magnetic resonance spectroscopy. J. Mol. Biol. 1986, 191:553-561.
    • (1986) J. Mol. Biol. , vol.191 , pp. 553-561
    • Clore, G.M.1    Martin, S.R.2    Gronenborn, A.M.3
  • 108
    • 0027373362 scopus 로고
    • Applications of nuclear magnetic resonance, circular dichroism and fluorescence spectroscopy to the characterization of biological products
    • Jones C. Applications of nuclear magnetic resonance, circular dichroism and fluorescence spectroscopy to the characterization of biological products. Biologicals 1993, 21:119-124.
    • (1993) Biologicals , vol.21 , pp. 119-124
    • Jones, C.1
  • 109
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Böhm G., Muhr R., Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 1992, 5:191-195.
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 110
    • 41049088527 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies
    • Doglia S.M., Ami D., Natalello A., Gatti-Lafranconi P., Lotti M. Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies. Biotechnol. J. 2008, 3:193-201.
    • (2008) Biotechnol. J. , vol.3 , pp. 193-201
    • Doglia, S.M.1    Ami, D.2    Natalello, A.3    Gatti-Lafranconi, P.4    Lotti, M.5
  • 111
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence Spectroscopy in Peptide and Protein Analysis
    • John Wiley & Sons, Ltd.
    • Ladokhin A.S. Fluorescence Spectroscopy in Peptide and Protein Analysis. Encyclopedia of Analytical Chemistry 2006, John Wiley & Sons, Ltd.
    • (2006) Encyclopedia of Analytical Chemistry
    • Ladokhin, A.S.1
  • 112
    • 22444436718 scopus 로고    scopus 로고
    • Single-molecule fluorescence spectroscopy of protein folding
    • Schuler B. Single-molecule fluorescence spectroscopy of protein folding. ChemPhysChem 2005, 6:1206-1220.
    • (2005) ChemPhysChem , vol.6 , pp. 1206-1220
    • Schuler, B.1
  • 113
    • 70449442780 scopus 로고    scopus 로고
    • Principles of fluorescent spectroscopy, third edition
    • Lakowicz J.R., Masters B.R. Principles of fluorescent spectroscopy, third edition. J. Biomed. Opt. 2008, 13:1-2.
    • (2008) J. Biomed. Opt. , vol.13 , pp. 1-2
    • Lakowicz, J.R.1    Masters, B.R.2
  • 114
    • 84859093147 scopus 로고    scopus 로고
    • Characterization of unstable hemoglobin A1c complexes by dynamic capillary isoelectric focusing
    • Hempe J.M., McGehee A.M., Hsia D., Chalew S.A. Characterization of unstable hemoglobin A1c complexes by dynamic capillary isoelectric focusing. Anal. Biochem. 2012, 424:149-155.
    • (2012) Anal. Biochem. , vol.424 , pp. 149-155
    • Hempe, J.M.1    McGehee, A.M.2    Hsia, D.3    Chalew, S.A.4
  • 115
    • 13444256353 scopus 로고    scopus 로고
    • Protocol of capillary isoelectric focusing to separate extremely acidic and basic proteins
    • Yang C., Zhang W., Zhang J., Duan J., Zhang Y. Protocol of capillary isoelectric focusing to separate extremely acidic and basic proteins. J. Sep. Sci. 2005, 28:78-86.
    • (2005) J. Sep. Sci. , vol.28 , pp. 78-86
    • Yang, C.1    Zhang, W.2    Zhang, J.3    Duan, J.4    Zhang, Y.5
  • 116
    • 0027908505 scopus 로고
    • Field-flow fractionation: analysis of macromolecular, colloidal, and particulate materials
    • Giddings J. Field-flow fractionation: analysis of macromolecular, colloidal, and particulate materials. Science 1993, 260:1456-1465.
    • (1993) Science , vol.260 , pp. 1456-1465
    • Giddings, J.1
  • 117
    • 0034284076 scopus 로고    scopus 로고
    • Fusion induced aggregation of model vesicles studied by dynamic and static light scattering
    • Trivedi V.D., Yu C., Veeramuthu B., Francis S., Chang D.K. Fusion induced aggregation of model vesicles studied by dynamic and static light scattering. Chem. Phys. Lipids 2000, 107:99-106.
    • (2000) Chem. Phys. Lipids , vol.107 , pp. 99-106
    • Trivedi, V.D.1    Yu, C.2    Veeramuthu, B.3    Francis, S.4    Chang, D.K.5
  • 118
    • 0042202405 scopus 로고    scopus 로고
    • Analysis for residual host cell proteins and DNA in process streams of a recombinant protein product expressed in Escherichia coli cells
    • Rathore A.S., Sobacke S.E., Kocot T.J., Morgan D.R., Dufield R.L., Mozier N.M. Analysis for residual host cell proteins and DNA in process streams of a recombinant protein product expressed in Escherichia coli cells. J. Pharm. Biomed. Anal. 2003, 32:1199-1211.
    • (2003) J. Pharm. Biomed. Anal. , vol.32 , pp. 1199-1211
    • Rathore, A.S.1    Sobacke, S.E.2    Kocot, T.J.3    Morgan, D.R.4    Dufield, R.L.5    Mozier, N.M.6
  • 119
    • 0036605742 scopus 로고    scopus 로고
    • An enzyme-linked immunosorbent assay for host cell protein contaminants in recombinant PEGylated staphylokinase mutant SY161
    • Wan M., Wang Y., Rabideau S., Moreadith R., Schrimsher J., Conn G. An enzyme-linked immunosorbent assay for host cell protein contaminants in recombinant PEGylated staphylokinase mutant SY161. J. Pharm. Biomed. Anal. 2002, 28:953-963.
    • (2002) J. Pharm. Biomed. Anal. , vol.28 , pp. 953-963
    • Wan, M.1    Wang, Y.2    Rabideau, S.3    Moreadith, R.4    Schrimsher, J.5    Conn, G.6
  • 120
    • 28444439937 scopus 로고    scopus 로고
    • A quantitative slot blot assay for host cell protein impurities in recombinant proteins expressed in E. coli
    • Zhu D., Saul A.J., Miles A.P. A quantitative slot blot assay for host cell protein impurities in recombinant proteins expressed in E. coli. J. Immunol. Methods 2005, 306:40-50.
    • (2005) J. Immunol. Methods , vol.306 , pp. 40-50
    • Zhu, D.1    Saul, A.J.2    Miles, A.P.3
  • 121
    • 0027304464 scopus 로고
    • Identification of an Escherichia coli protein impurity in preparations of a recombinant pharmaceutical
    • O'Keefe D.O., DePhillips P., Will M.L. Identification of an Escherichia coli protein impurity in preparations of a recombinant pharmaceutical. Pharm. Res. 1993, 10:975-979.
    • (1993) Pharm. Res. , vol.10 , pp. 975-979
    • O'Keefe, D.O.1    DePhillips, P.2    Will, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.