Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature
- 1 June 2006
- journal article
- Published by Elsevier in Journal of Chromatography B
- Vol. 837 (1-2), 35-43
- https://doi.org/10.1016/j.jchromb.2006.03.053
Abstract
No abstract availableThis publication has 36 references indexed in Scilit:
- Structural characterization of the maytansinoid–monoclonal antibody immunoconjugate, huN901–DM1, by mass spectrometryProtein Science, 2005
- The Rho-deamidating Cytotoxic Necrotizing Factor 1 fromEscherichia coli Possesses Transglutaminase ActivityJournal of Biological Chemistry, 1998
- Crystallographic structure of an intact IgG1 monoclonal antibody 1 1Edited by I. A. WilsonJournal of Molecular Biology, 1998
- Monitoring of IgG Antibody Thermal Stability by Micellar Electrokinetic Capillary Chromatography and Matrix-Assisted Laser Desorption/Ionization Mass SpectrometryAnalytical Chemistry, 1995
- Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl‐ and aspartyl‐containing peptidesInternational Journal of Peptide and Protein Research, 1995
- Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues: Effects of the solvent dielectricProtein Science, 1993
- Nonenzymatic Deamidation of Asparaginyl and Glutaminyl Residues in ProteinCritical Reviews in Biochemistry and Molecular Biology, 1991
- II. Aplysia brasiliana neurons R3–R14: Primary structure of the myoactive histidine-rich basic peptide and its prohormonePeptides, 1989
- Relative susceptibilities of the interchain disulfides of an immunoglobulin G molecule to reduction by dithiothreitolBiochemistry, 1977
- Rates of nonenzymic deamidation of glutaminyl and asparaginyl residues in pentapeptidesJournal of the American Chemical Society, 1973