A rapid method for relative quantification of N-glycans from a therapeutic monoclonal antibody during trastuzumab biosimilar development.

ABSTRACT: Glycosylation is a common post-translational modification and critical quality attribute that can modulate the efficacy of therapeutic proteins. In the production of monoclonal antibodies (mAbs), quantifying the glycoform profile is a vital characterization step. Traditional glycan analysis is time consuming and involves steps at extreme temperature or pH, which may alter glycans. Here, we describe a rapid method for glycan analysis in which glycans are released from mAb samples that are bound to protein A columns. Since host cell proteins, which may also contain glycans, were already removed, this step enables analysis of cell culture products. Glycans released from the mAb samples are then derivatized with InstantPC™ labeling agent and analyzed by HILIC-FLD-MS. To illustrate the method,

SUBMITTER: Segu Z 

PROVIDER: S-EPMC7188402 | biostudies-literature | 2020 Jan-Dec

REPOSITORIES: biostudies-literature