Monitoring Recombinant Glycoprotein Heterogeneity

Developing protein-based therapeutic agents requires both product quality and consistency to be maintained throughout the development and implementation of the production process. Differences in host cell type, the physiological status of the cell, and protein structural constraints are known to result in variations in post-translational modifications, which can affect the bioactivity, receptor binding, susceptibility to proteolysis, immunogenicity, and clearance rate of a therapeutic recombinant protein in vivo (1 ). Glycosylation is the most extensive source of protein heterogeneity, and many recent developments in analytical biotechnology have enhanced the ability to monitor and structurally define changes in oligosaccharides associated with recombinant proteins.