Purification of monoclonal antibodies by hydrophobic interaction chromatography under no-salt conditions

mAbs

Volumn 5, Issue 5, 2013, Pages 795-800

  Ghose, Sanchayita ^a   Tao, Yinying ^a   Conley, Lynn ^a   Cecchini, Douglas ^b  

^a BIOGEN   (United States)

^b Cambridge Center Bio7 6   (United States)

Author keywords

Aggregates; Flowthrough; HIC; Monoclonal antibodies; No salt

Indexed keywords

AMMONIUM SULFATE; CELL PROTEIN; MONOCLONAL ANTIBODY; RESIN;

ARTICLE; HOST CELL; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; HYDROPHOBICITY; PH;

AGGREGATES; FLOWTHROUGH; HIC; MONOCLONAL ANTIBODIES; NO SALT;

AMMONIUM SULFATE; ANTIBODIES, MONOCLONAL; CHROMATOGRAPHY; CITRATES; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR WEIGHT; PHOSPHATES; POTASSIUM COMPOUNDS; REPRODUCIBILITY OF RESULTS; SALTS;

EID: 84883887875     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.25552     Document Type: Article

References (21)

1. Shukla AA, Thömmes J. Recent advances in largescale production of monoclonal antibodies and related proteins. Trends Biotechnol 2010; 28:253-61; PMID:20304511; http://dx.doi.org/10.1016/j. tibtech.2010.02.001
2. Cramer SM, Holstein MA. Downstream bioprocessing: recent advances and future promise. Curr Opin Chem Eng 2011; 1:27-37; http://dx.doi.org/10.1016/j. coche.2011.08.008
3. McCue JT, Engel P, Ng A, Macniven R, Thömmes J. Modeling of protein monomer/aggregate purification and separation using hydrophobic interaction chromatography. Bioprocess Biosyst Eng 2008; 31:261-75; PMID:18205016; http://dx.doi.org/10.1007/s00449-008-0200-1
4. Shukla AA, Hubbard B, Tressel T, Guhan S, Low D. Downstream processing of monoclonal antibodies-application of platform approaches. J Chromatogr B Analyt Technol Biomed Life Sci 2007; 848:28-39; PMID:17046339; http://dx.doi.org/10. 1016/j. jchromb.2006.09.026
5. Jiang C, Flansburg L, Ghose S, Jorjorian P, Shukla AA. Defining process design space for a hydrophobic interaction chromatography (HIC) purification step: application of quality by design (QbD) principles. Biotechnol Bioeng 2010; 107:985-97; PMID:20683852; http://dx.doi.org/10.1002/bit.22894
6. Lu Y, Williamson B, Gillespie R. Recent advancement in application of hydrophobic interaction chromatography for aggregate removal in industrial purification process. Curr Pharm Biotechnol 2009; 10:427-33; PMID:19519419; http://dx.doi. org/10.2174/138920109788488897
7. Nagrath D, Xia F, Cramer SM. Characterization and modeling of nonlinear hydrophobic interaction chromatographic systems. J Chromatogr A 2011; 1218:1219-26; PMID:21255785; http://dx.doi. org/10.1016/j.chroma.2010.12.111
8. Melander WR, Corradini D, Horváth CS. Saltmediated retention of proteins in hydrophobic interaction chromatography. Application of solvophobic theory. J Chromatogr 1984; 317:67-85; PMID:6530455; http://dx.doi.org/10.1016/ S0021-9673(01)91648-6
9. Liu HF, Ma J, Winter C, Bayer R. Recovery and purification process development for monoclonal antibody production. MAbs 2010; 2:480-99; PMID:20647768; http://dx.doi.org/10.4161/mabs.2.5.12645
10. Senczuk AM, Klinke R, Arakawa T, Vedantham G, Yigzaw Y. Hydrophobic interaction chromatography in dual salt system increases protein binding capacity. Biotechnol Bioeng 2009; 103:930-5; PMID:19382248; http://dx.doi.org/ 10.1002/bit.22313
11. Urmann M, Graalfs H, Joehnck M, Jacob LR, Frech C. Cation-exchange chromatography of monoclonal antibodies: Characterization of a novel stationary phase designed for production-scale purification. MAbs 2010; 2:395-404; PMID:20559022
12. Roemling R, Jungbauer A. Meeting report: 8th HIC/RPC bioseparation conference. Biotechnol J 2013; Apr
13. http://dx.doi.org/10.1002/biot.201300123. [Epub ahead of print].
14. Chen J, Tetrault J, Ley A. Comparison of standard and new generation hydrophobic interaction chromatography resins in the monoclonal antibody purification process. J Chromatogr A 2008; 1177:272-81; PMID:17709111; http://dx.doi.org/10.1016/j. chroma.2007.07.083
15. Ghose S, Jin M, Liu J, Hickey J. Integrated polishing steps for monoclonal antibody purification. In: Gottschalk U, ed. Process Scale Purification of Antibodies. New York: John Wiley & Sons, 2009:145-167.
16. Gagnon P. Polishing methods for monoclonal IgG purification. In: Shukla AA, Etzel MR, Gadam S, ed. Process Scale Bioseparations for the Biopharmaceutical Industry. New York: Taylor & Francis, 2006: 491-505.
17. Arakawa T, Tsumoto K, Nagase K, Ejima D. The effects of arginine on protein binding and elution in hydrophobic interaction and ion-exchange chromatography. Protein Expr Purif 2007; 54:110-6; PMID:17408966; http://dx.doi.org/10.1016/j.pep.2007.02.010
18. Tsumoto K, Ejima D, Nagase K, Arakawa T. Arginine improves protein elution in hydrophobic interaction chromatography. The cases of human interleukin-6 and activin-A. J Chromatogr A 2007; 1154:81-6; PMID:17449045; http://dx.doi.org/10.1016/j.chroma. 2007.02.061
19. Gagnon P. Technology trends in antibody purification. J Chromatogr A 2012; 1221:57-70; PMID:22071423; http://dx.doi.org/10.1016/j.chroma.2011.10.034
20. Kato Y, Nakamura K, Kitamura T, Hasegawa M, Sasaki H. Hydrophobic interaction chromatography at low salt concentration for the capture of monoclonal antibodies. J Chromatogr A 2004; 1036:45-50; PMID:15139412; http://dx.doi.org/10.1016/j.chroma. 2004.02.009
21. Shukla AA, Yigzaw Y. Modes of Preparative Chromatography. In: Shukla AA, Etzel MR, Gadam S, ed. Process Scale Bioseparations for the Biopharmaceutical Industry. New York: Taylor & Francis, 2006: 491-505.