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  • Title: Identification of N-terminal modification for recombinant monoclonal antibody light chain using partial reduction and quadrupole time-of-flight mass spectrometry.
    Author: Yu L, Remmele RL, He B.
    Journal: Rapid Commun Mass Spectrom; 2006; 20(24):3674-80. PubMed ID: 17117408.
    Abstract:
    Since most recombinant monoclonal antibodies (mAbs) contain glutamic acid or glutamate at their N-terminus, cyclization of these residues to form pyroglutamate is an important degradation pathway that often occurs in therapeutic mAb development. In this work, a rapid method was developed to determine pyroglutamate at the N-terminus of mAb light chain by liquid chromatography coupled with electrospray ionization on a quadrupole time-of-flight mass spectrometer (QTOF). High levels of pyroglutamate were found at the N-terminus of the light chain of a typical recombinant mAb. The quantitative results were comparable to those obtained with a more conventional peptide mapping method. The direct method outlined here can be used to evaluate the impact of N-terminal cyclization during the processing of recombinant mAbs.
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