Effect of sodium butyrate on the assembly, charge variants, and galactosylation of antibody produced in recombinant Chinese hamster ovary cells
Abstract
Sodium butyrate (NaBu) is known to increase the specific productivity of recombinant Chinese hamster ovary (rCHO) cells. To understand the effects of NaBu on the product quality, rCHO cells producing monoclonal antibody (Mab) were cultivated at various concentrations of NaBu (0 to 4 mM). NaBu increased correctly assembled Mab. In the absence of NaBu, the proportions of intact Mab (2H2L) and heavy chain dimer (2H) were 81 and 15 %. At 1 mM NaBu, the proportion of 2H2L increased to 93 %, whereas the proportion of 2H decreased to 2 %. No further increase in the proportion of 2H2L was obtained at a higher NaBu concentration. NaBu also affected the charge heterogeneity of Mab, which may affect the efficacy of Mab. The basic charge variants of Mabs increased with an increase in the NaBu concentration. In addition, NaBu affected the galactosylation of Mab negatively. Overall, the data obtained here show that NaBu used in rCHO cell cultures for improved Mab production affects certain quality aspects of Mab, in this case, the charge heterogeneity and galactosylation.
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In fed-batch cultures, the most common process strategies to arrest cell growth are reducing culture temperature from 37°C to 30-34°C or adding chemical agents such as sodium butyrate.
“In fed-batch cultures, the most common process strategies to arrest cell growth are by reducing the culture temperature from 37 • C to temperatures ranging from 30 • C to 34 • C, or through the addition of chemical agents such as sodium butyrate.[20]”
From Biomass specific perfusion rate as a control lever for the continuous manufacturing of biosimilar monoclonal antibodies from CHO cell cultures (2024) · cites this paper as [20]
Cites
Glycosylation as a strategy to improve antibody-based therapeutics
Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829 · see citing works
Antioxidants reduce endoplasmic reticulum stress and improve protein secretion
Malhotra, J. D., Miao, H. Z., Zhang, K., Wolfson, A., Pennathur, S., Pipe, S. W., & Kaufman, R. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809677105 · Cited by 672 · see citing works
Optimal and consistent protein glycosylation in mammalian cell culture
Hossler, P., Khattak, S. F., & Li, Z. J. (2009) · Glycobiology · doi:10.1093/glycob/cwp079 · Cited by 669 · see citing works
Therapeutic antibodies for human diseases at the dawn of the twenty-first century
Brekke, O. H., & Sandlie, I. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd984 · Cited by 552 · see citing works
Picioreanu, C., van Loosdrecht, M. C. M., & Heijnen, J. J. (1998) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19980405)58:1 · Cited by 509 · see citing works
Identification of multiple sources of charge heterogeneity in a recombinant antibody
Harris, R. J., Kabakoff, B., Macchi, F. D., Shen, F. J., Kwong, M. Y., Andya, J. D., Shire, S. J., Bjork, N., Tótpál, K., & Chen, A. B. (2001) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(00)00548-x · Cited by 501 · see citing works
Heterogeneity of Monoclonal Antibodies
Liu, H., Gaza‐Bulseco, G., Faldu, D., Chumsae, C. M., & Sun, J. (2007) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21180 · Cited by 482 · see citing works
Melnick, J., Dul, J. L., & Argon, Y. (1994) · Nature · doi:10.1038/370373a0 · Cited by 428 · see citing works
Khawli, L. A., Goswami, S., Hutchinson, R., Glover, Z. K., Yang, J., Wang, X., Yao, Z., Sreedhara, A., Cano, T., Tesar, D. B., et al. (2010) · mAbs · doi:10.4161/mabs.2.6.13333 · Cited by 420 · see citing works
Effects of Charge on Antibody Tissue Distribution and Pharmacokinetics
Boswell, C. A., Tesar, D. B., Mukhyala, K., Theil, F.-P., Fielder, P. J., & Khawli, L. A. (2010) · Bioconjugate Chemistry · doi:10.1021/bc100261d · Cited by 398 · see citing works
Heterogeneity of Monoclonal Antibodies Revealed by Charge-Sensitive Methods
Vlasak, J., & Ionescu, R. M. (2008) · Current Pharmaceutical Biotechnology · doi:10.2174/138920108786786402 · Cited by 260 · see citing works
Schlatter, S., Stansfield, S. H., Dinnis, D. M., Racher, A. J., Birch, J. R., & James, D. C. (2005) · Biotechnology Progress · doi:10.1021/bp049780w · Cited by 230 · see citing works
Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn
Pan, H., Chen, K. S.-M., Chu, L., Kinderman, F. S., Apostoł, I., & Huang, G. (2009) · Protein Science · doi:10.1002/pro.45 · Cited by 204 · see citing works
Harris, R. J., Shire, S. J., & Winter, C. (2004) · Drug Development Research · doi:10.1002/ddr.10344 · Cited by 198 · see citing works
Chumsae, C. M., Gaza‐Bulseco, G., Sun, J., & Liu, H. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.11.050 · Cited by 192 · see citing works
Butyrate-Induced Transcriptional Changes in Human Colonic Mucosa
Vanhoutvin, S. A. L. W., Troost, F. J., Hamer, H. M., Lindsey, P. J., Koek, G. H., Jonkers, D. M. A. E., Kodde, A., Venema, K., & Brummer, R. J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006759 · Cited by 170 · see citing works
Lin, H. Y., Masso‐Welch, P. A., Di, Y. P., Cai, J. W., Shen, J., & Subjeck, J. R. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.11.1109 · Cited by 161 · see citing works
Enhanced Production of Monomeric Interferon-β by CHO Cells through the Control of Culture Conditions
Rodriguez, J., Spearman, M., Huzel, N., & Butler, M. (2008) · Biotechnology Progress · doi:10.1021/bp049807b · Cited by 145 · see citing works
Hendrick, V., Winnepenninckx, P., Abdelkafi, C., Vandeputte, O. M., Cherlet, M., Marique, T., Renemann, G., Loa, A., Kretzmer, G., & Wérenne, J. (2001) · Cytotechnology · doi:10.1023/a:1014088919546 · Cited by 126 · see citing works
Reddy, P. S., Sparvoli, A., Fagioli, C., Fassina, G., & Sitia, R. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00561.x · Cited by 125 · see citing works
Jiang, Z., & Sharfstein, S. T. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21726 · Cited by 118 · see citing works
Nutrient deprivation induces autophagy as well as apoptosis in Chinese hamster ovary cell culture
Hwang, S. O., & Lee, G. M. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21589 · Cited by 112 · see citing works
Self-citationSynthesis of Excess Light Chains of Gamma Globulin by Rabbit Lymph Node Cells
Shapiro, A. L., Scharff, M. D., Maizel, J. V., & Uhr, J. W. (1966) · Nature · doi:10.1038/211243a0 · Cited by 107 · see citing works
Mimura, Y., Lund, J., Church, S., Dong, S., Li, J., Goodall, M. D., & Jefferis, R. (2001) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00308-2 · Cited by 103 · see citing works
Characterization of the basic charge variants of a human IgG1
Kaschak, T., Boyd, D., Lu, F., Derfus, G. E., Kluck, B., Nogal, B., Emery, C., Summers, C., Zheng, K., Bayer, R. J., et al. (2011) · mAbs · doi:10.4161/mabs.3.6.17959 · Cited by 97 · see citing works
Chang, M. ‐., Tsai, Y., Chen, Y., Chan, C.-C., Huang, C.-X., Lan, W. C., Lin, C., Lan, W. H., & Jeng, J. (2012) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2012.01504.x · Cited by 93 · see citing works
Louis, M., Rosato, R. R., Brault, L., Osbild, S., Battaglia, E., Yang, X.-H., Grant, S., & Bagrel, D. (2004) · International Journal of Oncology · doi:10.3892/ijo.25.6.1701 · Cited by 93 · see citing works
Sung, Y. H., Song, Y. J., Lim, S. W., Chung, J. Y., & Lee, G. M. (2004) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2004.05.003 · Cited by 92 · see citing works
Self-citationChotigeat, W., Watanapokasin, Y., Mahler, S. M., & Gray, P. P. (1994) · Cytotechnology · doi:10.1007/bf00762396 · Cited by 92 · see citing works
Assembly of Immunoglobulin Light Chains as a Prerequisite for Secretion
Leitzgen, K., Knittler, M. R., & Haas, I. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.3117 · Cited by 89 · see citing works
Kim, N. S., & Lee, G. M. (2002) · Biotechnology and Bioengineering · doi:10.1002/bit.10191 · Cited by 86 · see citing works
Self-citationZhang, T., Bourret, J., & Cano, T. (2011) · Journal of Chromatography A · doi:10.1016/j.chroma.2011.05.061 · Cited by 81 · see citing works
Sung, Y. H., & Lee, G. M. (2005) · Biotechnology Progress · doi:10.1021/bp049892n · Cited by 56 · see citing works
Self-citationSantell, L., Ryll, T., Etcheverry, T., Santoris, M., Dutina, G., Wang, A., Gunson, J., & Warner, T. G. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0550 · Cited by 48 · see citing works
Effect of sodium butyrate on autophagy and apoptosis in Chinese hamster ovary cells
Lee, J. S., & Lee, G. M. (2011) · Biotechnology Progress · doi:10.1002/btpr.1512 · Cited by 45 · see citing works
Self-citationYoon, S., Hong, J. K., & Lee, G. M. (2004) · Biotechnology Progress · doi:10.1021/bp034382z · Cited by 36 · see citing works
Self-citationGlycosylation causes an apparent block in translation of immunoglobulin heavy chain.
Bergman, L. W., Harris, E., & Kuehl, W. M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70031-3 · Cited by 32 · see citing works
Lee, S., Kim, Y., Lee, E. G., & Lee, G. M. (2013) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2013.12.001 · Cited by 23 · see citing works
Self-citationHong, J. K., Lee, G. M., & Yoon, S. K. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.06.020 · Cited by 22 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Molecular and functional analysis of monoclonal antibodies in support of biologics development
Wang, X., An, Z., Luo, W., Xia, N., & Zhao, Q. (2017) · Protein & Cell · doi:10.1007/s13238-017-0447-x · Cited by 82 · see citing works
Park, J. H., Noh, S. M., Woo, J. R., Kim, J. W., & Lee, G. M. (2016) · Biotechnology Journal · doi:10.1002/biot.201500327 · Cited by 81 · see citing works
Self-citationHa, T. K., Kim, D., Kim, C. L., Grav, L. M., & Lee, G. M. (2022) · Biotechnology Advances · doi:10.1016/j.biotechadv.2021.107831 · Cited by 74 · see citing works
Self-citationMain Quality Attributes of Monoclonal Antibodies and Effect of Cell Culture Components
Torkashvand, F., & Vaziri, B. (2017) · Iranian Biomedical Journal · doi:10.18869/acadpub.ibj.21.3.131 · Cited by 72 · see citing works
Industrial bioprocessing perspectives on managing therapeutic protein charge variant profiles
Chung, S., Tian, J., Tan, Z., Chen, J., Lee, J., Borys, M., & Li, Z. J. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26587 · Cited by 66 · see citing works
Glycosylation of monoclonal antibody products: Current status and future prospects
Batra, J., & Rathore, A. S. (2016) · Biotechnology Progress · doi:10.1002/btpr.2366 · Cited by 64 · see citing works
Ribosome profiling-guided depletion of an mRNA increases cell growth rate and protein secretion
Kallehauge, T. B., Li, S., Pedersen, L. E., Ha, T. K., Ley, D., Andersen, M. R., Kildegaard, H. F., Lee, G. M., & Lewis, N. E. (2017) · Scientific Reports · doi:10.1038/srep40388 · Cited by 57 · see citing works
Self-citationOptimizing antibody expression: The nuts and bolts
Ayyar, B. V., Arora, S., & Ravi, S. S. (2017) · Methods · doi:10.1016/j.ymeth.2017.01.009 · Cited by 46 · see citing works
Fischer, S., Paul, A. J., Wagner, A., Mathias, S., Geiss, M., Schandock, F., Domnowski, M., Zimmermann, J., Handrick, R., Hesse, F., et al. (2015) · Biotechnology and Bioengineering · doi:10.1002/bit.25626 · Cited by 45 · see citing works
Majumdar, S., Desai, R., Hans, A. K., Dandekar, P. P., & Jain, R. D. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01060-6 · Cited by 43 · see citing works
Risk-Based Control Strategies of Recombinant Monoclonal Antibody Charge Variants
Beck, A., Nowak, C., Meshulam, D., Reynolds, K., Chen, D. J., Pacardo, D. B., Nicholls, S. B., Carven, G. J., Gu, Z., Fang, J., et al. (2022) · Antibodies · doi:10.3390/antib11040073 · Cited by 43 · see citing works
Park, J. H., Lim, J., Woo, J. R., Kim, J., & Lee, G. M. (2016) · Biotechnology Progress · doi:10.1002/btpr.2287 · Cited by 42 · see citing works
Self-citationRapid intensification of an established CHO cell fed‐batch process
Schulze, M., Niemann, J., Wijffels, R. H., Matuszczyk, J., & Martens, D. E. (2021) · Biotechnology Progress · doi:10.1002/btpr.3213 · Cited by 33 · see citing works
Zinc supplementation decreases galactosylation of recombinant IgG in CHO cells
Prabhu, A., Gadre, R. V., & Gadgil, M. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9064-8 · Cited by 32 · see citing works
Ha, T. K., Hansen, A. H., Kildegaard, H. F., & Lee, G. M. (2019) · Biotechnology Journal · doi:10.1002/biot.201900130 · Cited by 30 · see citing works
Self-citationQin, J., Wu, X. X., Xia, Z., Huang, Z., Zhang, Y., Wang, Y., Fu, Q., & Zheng, C. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9555-7 · Cited by 28 · see citing works
Madabhushi, S. R., Podtelezhnikov, A. A., Murgolo, N., Xu, S., & Lin, H. (2021) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2021.01.023 · Cited by 27 · see citing works
Decoupling Growth and Protein Production in CHO Cells: A Targeted Approach
Donaldson, J., Dale, M. P., & Rosser, S. J. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.658325 · Cited by 26 · see citing works
Avello, V., Tapia, B., Vergara, M., Acevedo, C., Berríos, J., Reyes, J. G., & Altamirano, C. (2017) · Electronic Journal of Biotechnology · doi:10.1016/j.ejbt.2017.03.008 · Cited by 25 · see citing works
Combining Butyrated ManNAc with Glycoengineered CHO Cells Improves EPO Glycan Quality and Production
Wang, Q., Chung, C., Yang, W., Yang, G., Chough, S., Chen, Y., Yin, B., Bhattacharya, R., Hu, Y., Saeui, C. T., et al. (2018) · Biotechnology Journal · doi:10.1002/biot.201800186 · Cited by 24 · see citing works
Explainable AI for CHO cell culture media optimization and prediction of critical quality attribute
Gangwar, N., Keerthiveena, B., & Rathore, A. S. (2024) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-024-13147-w · Cited by 24 · see citing works
Ling, W. L. W. (2015) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.15.8 · Cited by 20 · see citing works
Xu, P., Xu, S., He, C., & Khetan, A. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107577 · Cited by 20 · see citing works
Toronjo‐Urquiza, L., Acosta‐Martin, A. E., James, D. C., Nagy, T., & Falconer, R. J. (2019) · Biotechnology Progress · doi:10.1002/btpr.2940 · Cited by 14 · see citing works
Kim, D., Yoon, C., & Lee, G. M. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.28013 · Cited by 11 · see citing works
Self-citationSchulze, M., Kumar, Y., Rattay, M., Niemann, J., Wijffels, R. H., & Martens, D. E. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28150 · Cited by 10 · see citing works
Rahimi-Zarchi, M., Shojaosadati, S. A., Amiri, M. M., Jeddi‐Tehrani, M., & Shokri, F. (2018) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-018-1927-y · Cited by 10 · see citing works
Recombinant antibodies aggregation and overcoming strategies in CHO cells
Xu, T., Zhang, J., Wang, T., & Wang, X. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11977-0 · Cited by 10 · see citing works
Liu, M., Wang, J., Tang, H., Li, F., Zhao, L., Wang, H., Zhou, Y., & Tan, W. (2018) · Biotechnology Letters · doi:10.1007/s10529-018-2606-4 · Cited by 9 · see citing works
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Yuan, J., Gao, D., Hu, F., Shi, Y., Wu, Z.-H., Hu, C., Huang, X., Fang, W., Zhang, H., & Wang, H. (2020) · Journal of Chromatography B · doi:10.1016/j.jchromb.2020.122485 · Cited by 8 · see citing works
Leong, J., Tang, W. Q., Chng, J., Ler, W. X., Manan, N. A., Sim, L. C., Zheng, Z. Y., Zhang, W., Walsh, I., Zijlstra, G., et al. (2024) · Biotechnology Journal · doi:10.1002/biot.202400092 · Cited by 7 · see citing works
Niu, H., Wang, J., Liu, M., Chai, M., Zhao, L., Liu, X., Li, F., & Tan, W. (2018) · Bioresources and Bioprocessing · doi:10.1186/s40643-018-0228-2 · Cited by 7 · see citing works
Enhancing recombinant antibody yield in Chinese hamster ovary cells
Yang, C.-H., Li, H., & Lo, S. (2024) · Tzu Chi Medical Journal · doi:10.4103/tcmj.tcmj_315_23 · Cited by 7 · see citing works
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Gangwar, N., Dixit, N., & Rathore, A. S. (2025) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-025-13405-5 · Cited by 7 · see citing works
NEMATPOUR, F., Mahboudi, F., Khalaj, V., Vaziri, B., Ahmadi, S., Ahmadi, M., Ebadat, S., & Davami, F. (2017) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1702-18 · Cited by 6 · see citing works
Fan, Y., Kildegaard, H. F., & Andersen, M. R. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6972-2_14 · Cited by 4 · see citing works
Bravo-Venegas, J., Rodriguez-Siza, J., Vergara, M., Torres, M., Dickson, A., Toledo, J. R., Molina, M. C., Hermoso, M. A., Berríos, J., & Altamirano, C. (2026) · mAbs · doi:10.1080/19420862.2026.2643039 · Cited by 3 · see citing works
Modulating antibody N-glycosylation through feed additives using a multi-tiered approach
Kranjc, J., Kramer, L., Mikelj, M., Anderluh, M., Pišlar, A. H., & Brinc, M. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1448925 · Cited by 3 · see citing works
SWATH-MS insights on sodium butyrate effect on mAbs production and redox homeostasis in CHO cells
Galli, M., Liu, L. C.-Y., Sim, K. H., Kok, Y. J., Wongtrakul‐Kish, K., Nguyen‐Khuong, T., Tate, S. A., & Bi, X. (2024) · AMB Express · doi:10.1186/s13568-024-01807-z · Cited by 2 · see citing works
Zhu, Z., Chen, X., Li, W., Zhuang, Y., Zhao, Y., & Wang, G. (2022) · doi:10.22541/au.165401290.04491126/v1 · Cited by 2 · see citing works
Process intensification for CHO cell biomanufacturing
Schulze, M. (2023) · doi:10.18174/585711 · Cited by 2 · see citing works
Cell line-specific impact of dexamethasone on the bioprocessing of Chinese hamster ovary cells
An, Y. B., Kang, D. E., Yoo, J., You, W., Baik, J. Y., & Hong, J. K. (2024) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-024-00100-x · Cited by 1 · see citing works
Self-citationLim, J.-A., Lim, J.-H., Lee, J.-H., Cheon, S., Lee, G., Kim, Z., & Kim, D. (2024) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-024-00105-6 · Cited by 1 · see citing works
Self-citationLi, W.-F., Sun, Y.-T., Xia, K.-J., Fan, Z., Mi, C., Ashraf, K., Aldahmash, W., Mohsin, A., Wang, T.-Y., & Guo, M. (2026) · New Biotechnology · doi:10.1016/j.nbt.2026.03.012
Ran, Q., & Tan, W. (2026) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2026.08.008
- Authors
- Hong, J. K., Lee, S. M., Kim, K.-Y., & Lee, G. M.
- Affiliations
- Korea Advanced Institute of Science and Technology (KR)
- Corresponding author
- Lee, Sang Min
- Lee, Gyun Min
- Venue
- Applied Microbiology and Biotechnology
- Published
- 2014-02-21
- Volume
- 98
- Issue
- 12
- Pages
- 5417-5425
- ISSN
- 0175-7598 (ISSN-L)
- 1432-0614
- OpenAlex
- W2010303718
- Cited by
- 46
- References
- 39
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 8 · 2023: 1 · 2022: 4 · 2021: 5 · 2020: 2 · 2019: 2 · 2018: 8 · 2017: 7 · 2016: 2 · 2015: 3
- FWCI
- 1.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Applied Microbiology and Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Knowledge Economy
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Keywords
- sodium butyrate, monoclonal antibodies, antibody assembly, charge variants, galactosylation, antibody quality, product quality
- MeSH terms
- Animals, Antibodies, Monoclonal, Cricetulus, Galactose, Glycosylation, Cricetinae, Immunoglobulin Heavy Chains, Recombinant Proteins, CHO Cells, Protein Folding, Butyric Acid
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