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The study of protein  N -glycosylation is essential in biological and biopharmaceutical research as  N -glycans have been reported to regulate a wide range of physiological and pathological processes. Monitoring glycosylation in diagnosis, prognosis, as well as biopharmaceutical development and quality control are important research areas. A number of techniques for the analysis of protein  N -glycosylation are currently available. Here we examine three methodologies routinely used for the release of  N -glycans, in the effort to establish and standardize glycoproteomics technologies for quantitative glycan analysis from cultured cell lines.  N -glycans from human gamma immunoglobulins (IgG), plasma and a pool of four cancer cell lines were released following three approaches and the performance of each method was evaluated.

Method comparison for N-glycan profiling: Towards the standardization of glycoanalytical technologies for cell line analysis