Impact of ionic strength on adsorption capacity of chromatographic particles employed in separation of monoclonal antibodies

Chemical Papers

Volumn 64, Issue 4, 2010, Pages 461-468

  Wrzosek, Katarzyna ^a   Gramblička, Michal ^a   Tóthová, Darina ^a   Antošová, Monika ^a   Polakovič, Milan ^a  

^a SLOVAK UNIVERSITY OF TECHNOLOGY   (Slovakia)

Author keywords

Adsorption capacity; Cation exchange chromatography; Hydrophobic charge induction chromatography; Ionic strength; Monoclonal antibody; pH effect; Protein A chromatography; Stoichiometric model

Indexed keywords

EID: 77952290093     PISSN: 03666352     EISSN: 13369075     Source Type: Journal    
DOI: 10.2478/s11696-010-0019-5     Document Type: Article

References (31)

1. Barrande, M., Beurroies, I., Denoyel, R., Tatárová, I., Gramblička, M., Polakovič, M., Joehnck, M., & Schulte, M. (2009). Characterisation of porous materials for bioseparation. Journal of Chromatography A, 1216, 6906-6916. DOI: 10. 1016/j. chroma. 2009. 07. 075.
2. Boschetti, E. (2002). Antibody separation by hydrophobic charge induction chromatography. Trends in Biotechnology, 20, 333-337. DOI: 10. 1016/S0167-7799(02)01980-7.
3. Burton, S. C., & Harding, D. R. K. (1998). Hydrophobic charge induction chromatography: salt independent protein adsorption and facile elution with aqueous buffers. Journal of Chromatography A, 814, 71-81. DOI: 10. 1016/S0021-9673(98)00436-1.
4. Carter-Franklin, N., Victa, C., McDonald, P., & Fahrner, R. (2007). Fragments of protein A eluted during protein A affinity chromatography. Journal of Chromatography A, 1163, 105-111. DOI: 10. 1016/j. chroma. 2007. 06. 012.
5. Chen, J., Tetrault, J., & Ley, A. (2008). Comparison of standard and new generation hydrophobic interaction chromatography resins in the monoclonal antibody purification process. Journal of Chromatography A, 1177, 272-281. DOI: 10. 1016/j. chroma. 2007. 07. 083.
6. Denton, G., Murray, A., Price, M. R., & Levison, P. R. (2001). Direct isolation of monoclonal antibodies from tissue culture supernatant using the cation-exchange cellulose Express-Ion S. Journal of Chromatography A, 908, 223-234. DOI: 10. 1016/S0021-9673(00)00834-7.
7. Faude, A., Zacher, D., Müller, E., & Böttinger, H. (2007). Fast determination of conditions for maximum dynamic capacity in cation-exchange chromatography of human monoclonal antibodies. Journal of Chromatography A, 1161, 29-35 DOI: 10. 1016/j. chroma. 2007. 03. 114.
8. Follman, D. K., & Fahrner, R. L. (2004). Factorial screening of antibody purification processes using three chromatography steps without protein A. Journal of Chromatography A, 1024, 79-85. DOI: 10. 1016/j. chroma. 2003. 10. 060.
9. Forrer, N., Butté, A., & Morbidelli, M. (2008). Chromatographic behavior of a polyclonal antibody mixture on a strong cation exchanger column. Part I: Adsorption characterization Journal of Chromatography A, 1214, 59-70. DOI: 10. 1016/j. chroma. 2008. 10. 048.
10. Ghose, S., Hubbard, B., & Cramer, S. M. (2006). Evaluation and comparison of alternatives to Protein A chromatography: Mimetic and hydrophobic charge induction chromatographic stationary phases. Journal of Chromatography A, 1122, 144-152. DOI: 10. 1016/j. chroma. 2006. 04. 083.
11. Gramblička, M., Tóthová, D., Antošová, M., & Polakovič, M. (2008). Influence of pH on adsorption of human immunoglobulin gamma, human serum albumin and horse myoglobin by commercial chromatographic materials designed for downstream processing of monoclonal antibodies. Acta Chimica Slovaca, 1(1) 85-94.
12. Guerrier, L., Flayeux, I., & Boschetti, E. (2001). A dual-mode approach to the selective separation of antibodies and their fragments. Journal of Chromatography B, 755, 37-46. DOI: 10. 1016/S0378-4347(00)00598-3.
13. Hahn, R., Schlegel, R., & Jungbauer, A. (2003). Comparison of protein A affinity sorbents. Journal of Chromatography B, 790, 35-51. DOI: 10. 1016/S1570-0232(03)00092-8.
14. Hahn, R., Shimahara, K., Steindl, F., & Jungbauer, A. (2006). Comparison of protein A affinity sorbents III. Life time study. Journal of Chromatography A, 1102, 224-231. DOI: 10. 1016/j. chroma. 2005. 10. 083.
15. Hober, S., Nord, K., & Linhult, M. (2007). Protein A chromatography for antibody purification. Journal of Chromatography B, 848, 40-47. DOI: 10. 1016/j. jchromb. 2006. 09. 030.
16. Huse, K., Böhme, H.-J., & Scholz, G. H. (2002). Purification of antibodies by affinity chromatography. Journal of Biochemical and Biophysical Methods, 51, 217-231. DOI: 10. 1016/S0165-022X(02)00017-9.
17. Jungbauer, A. (2005). Chromatographic media for bioseparation. Journal of Chromatography A, 1065, 3-12. DOI: 10. 1016/j. chroma. 2004. 08. 162.
18. Low, D., O'Leary, R., & Pujar, N. S. (2007). Future of antibody purification. Journal of Chromatography B, 848, 48-63. DOI: 10. 1016/j. jchromb. 2006. 10. 033.
19. Mollerup, J. M. (2006). Applied thermodynamics: A new frontier for biotechnology. Fluid Phase Equilibria, 241, 205-215. DOI: 10. 1016/j. fluid. 2005. 12. 037.
20. Necina, R., Amatschek, K., & Jungbauer, A. (1998). Capture of human monoclonal antibodies from cell culture supernatant by ion exchange media exhibiting high charge density. Biotechnology and Bioengineering, 60, 689-698. DOI: 10. 1002/(SICI)1097-0290(19981220)60: 6〈689:: AID-BIT6〉3. 0. CO; 2-M.
21. Okay, O. (2000). Macroporous copolymer networks. Progress in Polymer Science, 25, 711-779. DOI: 10. 1016/S0079-6700(00)00015-0.
22. Roque, A. C. A., Silva, C. S. O., & Taipa, M. Á. (2007). Affinitybased methodologies and ligands for antibody purification: Advances and perspectives. Journal of Chromatography A, 1160, 44-55. DOI: 10. 1016/j. chroma. 2007. 05. 109.
23. Schwartz, W., Judd, D., Wysocki, M., Guerrier, L., Birck-Wilson, E., & Boschetti, E. (2001). Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies. Journal of Chromatography A, 908, 251-263. DOI: 10. 1016/S0021-9673(00)01013-X.
24. Shukla, A. A., Hubbard, B., Tressel, T., Guhan, S., & Low, D. (2007). Downstream processing of monoclonal antibodies-Application of platform approaches. Journal of Chromatography B, 848, 28-39. DOI: 10. 1016/j. jchromb. 2006. 09. 026.
25. Smith, A. W. (1948). Elements of physics (5th ed.). New York, NY, USA: McGraw-Hill.
26. Staby, A., Jacobsen, J. H., Hansen, R. G., Bruus, U. K., & Holm Jensen, I. (2006). Comparison of chromatographic ion-exchange resins: V. Strong and weak cation-exchange resins. Journal of Chromatography A, 1118, 168-179. DOI: 10. 1016/j. chroma. 2006. 03. 116.
27. Staby, A., Sand, M.-B., Hansen, R. G., Jacobsen, J. H., Andersen, L. A., Gerstenberg, M., Bruus, U. K., & Holm Jensen, I. (2005). Comparison of chromatographic ion-exchange resins: IV. Strong and weak cation-exchange resins and heparin resins. Journal of Chromatography A, 1069, 65-77. DOI: 10. 1016/j. chroma. 2004. 11. 094.
28. Stone, M. C., Tao, Y., & Carta, G. (2009). Protein adsorption and transport in agarose and dextran-grafted agarose media for ion exchange chromatography: Effect of ionic strength and protein characteristics. Journal of Chromatography A, 1216, 4465-4474. DOI: 10. 1016/j. chroma. 2009. 03. 044.
29. Tatárová, I., Gramblička, M., Antošová, M., & Polakovič, M. (2008). Characterization of pore structure of chromatographic adsorbents employed in separation of monoclonal antibodies using size-exclusion techniques. Journal of Chromatography A, 1193, 129-135. DOI: 10. 1016/j. chroma. 2008. 04. 023.
30. Tugcu, N., Bae, S. S., Moore, J. A., & Cramer, S. M. (2002). Stationary phase effects on the dynamic affinity of lowmolecular-mass displacers. Journal of Chromatography A, 954, 127-135. DOI: 10. 1016/S0021-9673(02)00164-4.
31. Zhu-Shimoni, J., Gunawan, F., Thomas, A., Vanderlaan, M., & Stults, J. (2009). Trace level analysis of leached Protein A in bioprocess samples without interference from the large excess of rhMAb IgG. Journal of Immunological Methods, 341, 59-67. DOI: 10. 1016/j. jim. 2008. 10. 015.