Wakankar et al., 2007 - Google Patents
Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodiesWakankar et al., 2007
- Document ID
- 13305002119923764958
- Author
- Wakankar A
- Borchardt R
- Eigenbrot C
- Shia S
- Wang Y
- Shire S
- Liu J
- Publication year
- Publication venue
- Biochemistry
External Links
Snippet
The aspartic acid residues (Asp) present in the complementarity-determining regions (CDRs) of the light chains of two recombinant monoclonal antibodies (MAbs), MAb I and MAb II, are highly susceptible to isomerization due to the presence of glycine residues (Gly) …
- 108010045030 monoclonal antibodies 0 title abstract description 373
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
- G01N30/86—Signal analysis
- G01N30/8665—Signal analysis for calibrating the measuring apparatus
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
- G01N30/62—Detectors specially adapted therefor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Wakankar et al. | Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies | |
Cacia et al. | Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: identification and effect on binding affinity | |
Xu et al. | Structure, heterogeneity and developability assessment of therapeutic antibodies | |
Füssl et al. | Charge variant analysis of monoclonal antibodies using direct coupled pH gradient cation exchange chromatography to high-resolution native mass spectrometry | |
Huang et al. | In vivo deamidation characterization of monoclonal antibody by LC/MS/MS | |
Haberger et al. | Assessment of chemical modifications of sites in the CDRs of recombinant antibodies: Susceptibility vs. functionality of critical quality attributes | |
Bults et al. | LC-MS/MS-based monitoring of in vivo protein biotransformation: quantitative determination of trastuzumab and its deamidation products in human plasma | |
Wei et al. | Native hydrophobic interaction chromatography hyphenated to mass spectrometry for characterization of monoclonal antibody minor variants | |
Beyer et al. | Microheterogeneity of recombinant antibodies: analytics and functional impact | |
D’Atri et al. | Hydrophilic interaction chromatography hyphenated with mass spectrometry: a powerful analytical tool for the comparison of originator and biosimilar therapeutic monoclonal antibodies at the middle-up level of analysis | |
Houde et al. | Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry | |
Zhang et al. | Identification and characterization of buried unpaired cysteines in a recombinant monoclonal IgG1 antibody | |
Jung et al. | Physicochemical characterization of Remsima® | |
Rea et al. | Validation of a pH gradient-based ion-exchange chromatography method for high-resolution monoclonal antibody charge variant separations | |
Hernandez-Alba et al. | Native mass spectrometry, ion mobility, and collision-induced unfolding for conformational characterization of IgG4 monoclonal antibodies | |
Miller et al. | Characterization of site-specific glycation during process development of a human therapeutic monoclonal antibody | |
Camperi et al. | Fast and automated characterization of monoclonal antibody minor variants from cell cultures by combined protein-A and multidimensional LC/MS methodologies | |
Ponniah et al. | Characterization of the acidic species of a monoclonal antibody using weak cation exchange chromatography and LC-MS | |
Pan et al. | Subzero temperature chromatography and top-down mass spectrometry for protein higher-order structure characterization: method validation and application to therapeutic antibodies | |
Neill et al. | Characterization of recombinant monoclonal antibody charge variants using OFFGEL fractionation, weak anion exchange chromatography, and mass spectrometry | |
Hamuro | Tutorial: chemistry of hydrogen/deuterium exchange mass spectrometry | |
Alam et al. | Deamidation can compromise antibody colloidal stability and enhance aggregation in a pH-dependent manner | |
Zhang et al. | Structural and functional characterization of a hole–hole homodimer variant in a “knob-into-hole” bispecific antibody | |
Limpikirati et al. | Covalent labeling and mass spectrometry reveal subtle higher order structural changes for antibody therapeutics | |
Zhang et al. | Structural changes and aggregation mechanisms of two different dimers of an IgG2 monoclonal antibody |