2004
DOI: 10.1016/j.jchromb.2004.01.029
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Aggregation and denaturation of antibodies: a capillary electrophoresis, dynamic light scattering, and aqueous two-phase partitioning study

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Cited by 53 publications
(31 citation statements)
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References 29 publications
(34 reference statements)
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“…11B), which had a hydrodynamic size (5.3 nM) comparable to previously reported values for other IgG molecules. [39][40][41][42][43] Homology modeling suggested that the succinimide intermediate is stabilized via π interaction with the side chain of an adjacent tryptophan residue. Using SPR analysis, we found a moderate decrease in binding affinity of mAb-1, which contained one succinimide105 modification on the HC, compared with a fraction containing no modifications (HC Asn105).…”
Section: Discussionmentioning
confidence: 99%
“…11B), which had a hydrodynamic size (5.3 nM) comparable to previously reported values for other IgG molecules. [39][40][41][42][43] Homology modeling suggested that the succinimide intermediate is stabilized via π interaction with the side chain of an adjacent tryptophan residue. Using SPR analysis, we found a moderate decrease in binding affinity of mAb-1, which contained one succinimide105 modification on the HC, compared with a fraction containing no modifications (HC Asn105).…”
Section: Discussionmentioning
confidence: 99%
“…Monitoring of physical changes is represented by the application of CZE to investigate the aggregation process of b-amyloid peptides [273], and aggregation and denaturation of antibodies [274]. CZE separation of folded and unfolded forms of polypeptides and proteins allows studying the equilibria and kinetics of conformation transition states during polypeptide and protein folding/ unfolding/refolding processes [275].…”
Section: Monitoring Of Chemical and Enzymatical Reactions And Physicamentioning
confidence: 99%
“…CZE was used to study b-amyloid and its aggregation [275], botulinum neurotoxin B light chain activity [276], nonenzymatic posttranslation modifications on BSA [277], aminoacyl-tRNA synthetase localized in cell nucleus [278], protein-protein interactions [279], aggregation and denaturation of antibodies [280], glycosylation of murine erythropoietin [281], PEGylation of proteins [282], glutamine deamidation in proteins [283], complexation of apomyoglobin with Coumarin 153 [284], reaction of FQ with ovalbumin [285], interaction of GFP with calcium [286], noncovalent complexation in myoglobin [287], DNA-protein interactions [288][289][290], binding fucoidan to antithrombin [291], retinoic acid to b-lactoglobulin B [292], and binding phospholipid and glycosaminoglycan to human b 2 -glycoprotein [293].…”
Section: Other Proteinsmentioning
confidence: 99%