A high-throughput method for fast detecting unfolding of monoclonal antibodies on cation exchange resins
Published 2020 View Full Article
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Title
A high-throughput method for fast detecting unfolding of monoclonal antibodies on cation exchange resins
Authors
Keywords
Differential scanning fluorimetry, High-throughput measurement, Protein stability, Ion-exchange chromatography
Journal
JOURNAL OF CHROMATOGRAPHY A
Volume 1634, Issue -, Pages 461688
Publisher
Elsevier BV
Online
2020-11-11
DOI
10.1016/j.chroma.2020.461688
References
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Related references
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- Effects of salt-induced reversible self-association on the elution behavior of a monoclonal antibody in cation exchange chromatography
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- Unfolding of a model protein on ion exchange and mixed mode chromatography surfaces
- (2014) Adrian M. Gospodarek et al. JOURNAL OF CHROMATOGRAPHY A
- Unfolding and aggregation of a glycosylated monoclonal antibody on a cation exchange column. Part II. Protein structure effects by hydrogen deuterium exchange mass spectrometry
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- High-Throughput Thermal Scanning for Protein Stability: Making a Good Technique More Robust
- (2013) Shane A. Seabrook et al. ACS Combinatorial Science
- Cation exchange surface-mediated denaturation of an aglycosylated immunoglobulin (IgG1)
- (2012) Ron Gillespie et al. JOURNAL OF CHROMATOGRAPHY A
- Thermal Denaturation Assays in Chemical Biology
- (2011) Guillermo Senisterra et al. ASSAY AND DRUG DEVELOPMENT TECHNOLOGIES
- A high-throughput fluorescence chemical denaturation assay as a general screen for protein–ligand binding
- (2010) Kumaran Mahendrarajah et al. ANALYTICAL BIOCHEMISTRY
- Behavior of human serum albumin on strong cation exchange resins: II. Model analysis
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- Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
- (2010) Zhongqi Zhang et al. PROTEIN SCIENCE
- Hydrophobic interaction chromatography of proteins: Thermodynamic analysis of conformational changes
- (2009) Rene Ueberbacher et al. JOURNAL OF CHROMATOGRAPHY A
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