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Identification and Quantification of Protein Modifications by Peptide Mapping with UPLC/MSE
In this application note, we demonstrate the utility of UPLC/MSE for identification and quantification of covalent modifications in a yeast alcohol dehydrogenase (ADH) digest. The results presented here demonstrate application of UPLC/MSE for characterization of protein peptide maps. UPLC/MSE was successfully used for identification and quantification of modifications in ADH1. The stoichiometry of modifications ranged from 1% to 99%. UPLC/MSE, combining here the ACQUITY UPLC and SYNAPT MS systems, meets requirements for robust and flexible methods that are needed to monitor safety and stability of biopharmaceutical proteins.
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