ArticleBiochemical and biophysical research communications2018
Unfolding of IgG domains detected by non-reducing SDS-PAGE.
Article in Biochemical and biophysical research communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed.
- A Synthetic Platform for Antibody Junctional Diversification Beyond Natural Constraints.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Analytical Physicochemical and Functional Studies to Compare AryoTrust, a Follow-On Biologics, with the Originator Trastuzumab (Herceptin).Pharmaceutics · 2026Article
- Synthesis and characterization of a functional benzoylecgonine - bovine serum albumin conjugate for quantification of a humanized monoclonal anti-cocaine antibody.Biochemistry and biophysics reports · 2025Article
- Enhanced Detection of αGal Using a Novel Monoclonal IgG1 Antibody: Comparative Evaluation with IgM Antibody [Clone M86].Journal of personalized medicine · 2025Article
- Robust and Reproducible Monoclonal Antibody Production Using a Transgenic Silkworm System.International journal of molecular sciences · 2025Article
- Generation of Novel Monoclonal Antibodies Recognizing Rabbit CD34 Antigen.Biomolecules · 2025Article
- Optimization and Validation of the Cationization Method for the Fab' Fragment of Antibody Rituximab.ACS omega · 2025Article
- Human monoclonal antibody cloning and expression with overlap extension PCR and short DNA fragments.Journal of immunological methods · 2024Article
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- Tyrosine nitration of a humanized anti-cocaine mAb differentially affects ligand binding of cocaine and its metabolites.Biochemistry and biophysics reports · 2022Article
- Comparative analysis of plant transient expression vectors for targeted N-glycosylation.Frontiers in bioengineering and biotechnology · 2022Article
- Cocaine binding to the Fab fragment of a humanized anti-cocaine mAb quantitated by dye absorption and fluorescence spectroscopy.Journal of immunological methods · 2021Article
- Plant-made antibody against miroestrol: a new platform for expression of full-length immunoglobulin G against small-molecule targets in immunoassays.Plant cell reports · 2021Article
- Ligand binding to a humanized anti-cocaine mAb measured by dye absorption spectroscopy.Biochemical and biophysical research communications · 2021Article
- Multi-domain unfolding of the Fab fragment of a humanized anti-cocaine mAb characterized by non-reducing SDS-PAGE.Biochemical and biophysical research communications · 2020Article
- Ligand binding to a humanized anti-cocaine mAb detected by non-reducing SDS-PAGE.Biochemistry and biophysics reports · 2020Article
- Palmitoylation of Hepatitis C Virus NS2 Regulates Its Subcellular Localization and NS2-NS3 Autocleavage.Journal of virology · 2019Article
- Domain unfolding of monoclonal antibody fragments revealed by non-reducing SDS-PAGE.Biochemistry and biophysics reports · 2018Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Monoclonal antibodies are very important in modern therapeutics and constitute a substantial percentage of newly approved drugs. Every therapeutic monoclonal antibody must be analyzed for structural and functional integrity, and all protein heterogeneities need to be identified and quantified. The conformational stabilities of the monoclonal antibodies are also important for antibody storage and handling stabilities. One of the first and simplest of the structural analysis techniques utilized is SDS-PAGE, which can be performed both with and without prior reduction to break disulfide bonds. This permits sizing of both heavy and light chains in the reduced condition, and sizing of the intact antibody and any disulfide aggregates in the non-reduced condition. Analyzing our human anti-cocaine monoclonal antibody, we noted unexpectedly larger apparent molecular weights and apparent protein size heterogeneities using non-reducing SDS-PAGE. These apparent molecular weight heterogeneities are not consistent with other analysis techniques. Heterogeneities were noted using several heating and pre-electrophoretic sample preparation protocols, and are modified by the inclusion of small concentrations of certain alcohols such as propanol and butanol. All of these unexpected results were also observed for a commercial human IgG
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