A Novel, Site-Specific N-Linked Glycosylation Model Provides Mechanistic Insights Into the Process-Condition Dependent Distinct Fab and Fc Glycosylation of an IgG1 Monoclonal Antibody Produced by CHO VRC01 Cells.

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作者： Jayanth Venkatarama,Reddy ^[1] ; Thomas,Leibiger ^[1] ; Sumit Kumar,Singh ^[2] ; Kelvin H,Lee ^[1] ; Eleftherios,Papoutsakis ^[3] ; Marianthi,Ierapetritou ^[1]

作者单位： Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware, USA. ^[1] Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware, USA.;School of Biochemical Engineering, Indian Institute of Technology (Banaras Hindu University), Varanasi, India. ^[2] Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware, USA.;Delaware Biotechnology Institute, & Department of Biological Sciences, University of Delaware, Newark, Delaware, USA. ^[3]

关键词 Fab glycosylation critical process parameters critical quality attributes glycosylation model site‐specific N‐linked glycosylation

DOI 10.1002/bit.28916

PMID 39740206

发布时间 2024-12-31

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A Novel, Site-Specific N-Linked Glycosylation Model Provides Mechanistic Insights Into the Process-Condition Dependent Distinct Fab and Fc Glycosylation of an IgG1 Monoclonal Antibody Produced by CHO VRC01 Cells.

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A Novel, Site-Specific N-Linked Glycosylation Model Provides Mechanistic Insights Into the Process-Condition Dependent Distinct Fab and Fc Glycosylation of an IgG1 Monoclonal Antibody Produced by CHO VRC01 Cells.

Biotechnology and bioengineering

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