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Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry.
Ultrasonic Pretreatment Combined with Dry-State Glycation Reduced the Immunoglobulin E/Immunoglobulin G-Binding Ability of ?-Lactalbumin Revealed by High-Resolution Mass Spectrometry.
Influence of glycan modification on IgG1 biochemical and biophysical properties.
The mechanism of reduced IgG/IgE-binding of ?-lactoglobulin by pulsed electric field pretreatment combined with glycation revealed by ECD/FTICR-MS.
Mechanism of Reduction in IgG and IgE Binding of ?-Lactoglobulin Induced by Ultrasound Pretreatment Combined with Dry-State Glycation: A Study Using Conventional Spectrometry and High-Resolution Mass Spectrometry.
A systematic assessment of structural heterogeneity and IgG/IgE-binding of ovalbumin.
Extending the capabilities of intact-mass analyses to monoclonal immunoglobulins of the E-isotype (IgE).