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- W2048814278 endingPage "2447" @default.
- W2048814278 startingPage "2426" @default.
- W2048814278 abstract "Heterogeneity of monoclonal antibodies is common due to the various modifications introduced over the lifespan of the molecules from the point of synthesis to the point of complete clearance from the subjects. The vast number of modifications presents great challenge to the thorough characterization of the molecules. This article reviews the current knowledge of enzymatic and nonenzymatic modifications of monoclonal antibodies including the common ones such as incomplete disulfide bond formation, glycosylation, N-terminal pyroglutamine cyclization, C-terminal lysine processing, deamidation, isomerization, and oxidation, and less common ones such as modification of the N-terminal amino acids by maleuric acid and amidation of the C-terminal amino acid. In addition, noncovalent associations with other molecules, conformational diversity and aggregation of monoclonal antibodies are also discussed. Through a complete understanding of the heterogeneity of monoclonal antibodies, strategies can be employed to better identify the potential modifications and thoroughly characterize the molecules." @default.
- W2048814278 created "2016-06-24" @default.
- W2048814278 creator A5009963400 @default.
- W2048814278 creator A5040550871 @default.
- W2048814278 creator A5062252218 @default.
- W2048814278 creator A5087945394 @default.
- W2048814278 creator A5091595488 @default.
- W2048814278 date "2008-07-01" @default.
- W2048814278 modified "2023-10-17" @default.
- W2048814278 title "Heterogeneity of Monoclonal Antibodies" @default.
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