[A. K. Pavlou and J. M. Reichert, Recombinant protein therapeutics - success rates, market trends and values to 2010, Nature Biotechnol. 22 (2004) 1513-1519; DOI: 10.1038/nbt1204-1513.10.1038/nbt1204-1513]Search in Google Scholar
[A. C. Herman, T. C. Boone and S. Lu, Characterization, Formulation and Stability of Neupogen (Filgrastim), a Recombinant Human Granulocyte-colony Stimulating Factor, in Formulation, Characterization and Stability of Protein Drugs (Eds. R. Pearlman and Y. J. Wang), Plenum Press, New York 1996, pp. 303-328.10.1007/0-306-47452-2_7]Search in Google Scholar
[V. Gervais, A. Zerial and H. Oschkinat, NMR investigations of the role of the sugar moiety in glycosylated recombinant human G-CSF, Eur. J. Biochem. 247 (1997) 386-395.10.1111/j.1432-1033.1997.00386.x]Search in Google Scholar
[C. Wang, M. Eufemi, C. Turano and A. Giartosio, Influence of the carbohydrate moiety on the stability of glycoproteins, Biochemistry 35 (1996) 7299-7307; DOI: 10.1021/bi9517704.10.1021/bi9517704]Search in Google Scholar
[C. Nissen, Glycosylation of recombinant human granulocyte-colony stimulating factor: implications for stability and potency, Eur. J. Cancer 30A (Suppl. 3) (1994) S12-S14.]Search in Google Scholar
[M. Oheda, M. Hasegawa, K. Hattori, H. Kuboniwa, T. Kojima, T. Orita, K. Tomonou, T. Yamazaki and N. Ochi, O-linked sugar chain of hG-CSF protects it against polymerization and denaturation allowing it to retain its biological activity, J. Biol. Chem. 265 (1990) 11432-11436.10.1016/S0021-9258(19)38416-9]Search in Google Scholar
[A. Hüttmann, K. Schirsafi, S. Seeber and P. Bojko, Comparison of lenograstim and filgrastim: effects on blood cell recovery after high-dose chemotherapy and autologous peripheral blood stem cell transplantation, J. Cancer Res. Clin. Oncol. 131 (2005) 152-156; DOI: 10.1007/s00432-004-0636-x.10.1007/s00432-004-0636-x]Search in Google Scholar
[M. Hoglund, B. Smedmyr, M. Bengtsson, T. H. Totterman, U. Cour-Chabernaud and A. Yver, Mobilisation of CD34+ cells by glycosylated and non-glycosylated GSCF in healthy volunteers - A comparative study, Eur. J. Haematol. 59 (1997) 177-183.10.1111/j.1600-0609.1997.tb00972.x]Search in Google Scholar
[W. Wang, Instability, stabilization, and formulation of liquid protein pharmaceuticals, Int. J. Pharm. 185 (1999) 129-188; DOI: 10.1016/S0378-5173(99)00152-0.10.1016/S0378-5173(99)00152-0]Search in Google Scholar
[E. Y. Chi, S. Krishnan, B. S. Kendrick, B. S. Chang, J. F. Carpenter and T. W. Randolph, Roles of conformational stability and colloidal stability in the aggregation of rHuG-CSF, Protein Sci. 12 (2003) 903-913.10.1110/ps.0235703]Search in Google Scholar
[S. Krishnan, E. Y. Chi, J. N. Webb, B. S. Chang, D. Shan, M. Goldenberg, M. C. Manning, T. W. Randolph and J. F. Carpenter, Aggregation of G-CSF under physiological conditions: Characterization and thermodynamic inhibition, Biochemistry 41 (2002) 6422-6431; DOI: 10.1021/bi 012006m.]Search in Google Scholar
[M. W. Bruner, J. Goldstein, C. R. Middaugh, M. A. Brooks and D. B. Volkin, Size exclusion HPLC method for the determination of acidic fibroblast growth factor in viscous formulations, J. Pharm. Biomed. Anal. 15 (1997) 1929-1935; DOI: 10.1016/S0731-7085(96)02043-2.10.1016/S0731-7085(96)02043-2]Search in Google Scholar
[K. Ahrer, A. Buchacher, G. Iberer and A. Jungbauer, Detection of aggregate formation during production of human immunoglobulin G by means of light scattering, J. Chromatogr. A 1043 (2004) 41-46; DOI: 10.1016/j.chroma.2004.05.024.10.1016/j.chroma.2004.05.02415317411]Search in Google Scholar
[R. S. Gunturi, I. Ghobrial and B. Sharma, Development of a sensitive size exclusion HPLC method with fluorescence detection for the quantitation of rHuEPO aggregates, J. Pharm. Biomed. Anal. 43 (2007) 213-221; DOI: 10.1016/j.jpba.2006.06.006.10.1016/j.jpba.2006.06.00616875794]Search in Google Scholar
[J. P. Gabrielson, M. L. Brader, A. H. Pekar, K. B. Mathis, G. Winter, J. F. Carpenter and T. W. Randolph, Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation and sedimentation velocity, J. Pharm. Sci. 96 (2007) 268-279; DOI: 10.1002/jps.20760.10.1002/jps.2076017080424]Search in Google Scholar
[C. F. Codevilla, L. Brum, P. R. de Oliveira, C. Dolman, B. Rafferty and S. L. Dalmora, Validation of an SEC-HPLC method for the analysis of rhG-CSF in pharmaceutical formulation, J. Liq. Chrom. 27 (2004) 2689-2698; DOI: 10.1081/JLC-200029121.10.1081/JLC-200029121]Search in Google Scholar
[S. W. Raso, J. Abel, J. M. Barnes, K. M. Maloney, G. Pipes, M. J. Treuheit, J. King and D. N. Brems, Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state, Protein Sci. 14 (2005) 2246-2257; DOI: 10.1110/ps.051489405.10.1110/ps.051489405225347916131655]Search in Google Scholar
[U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685; DOI: 10.1038/227680a0.10.1038/227680a05432063]Search in Google Scholar
[M. E. Cromwell, E. Hilario and F. Jacobson, Protein aggregation and bioprocessing, AAPS Journal 8 (2006) E572-E579; DOI: 10.1208/aapsj080366.10.1208/aapsj080366276106417025275]Search in Google Scholar