earticle

영어

Glycosylation is one of the most important post-translational modifications of protein, which plays a key role on the stability and immunogenicity of therapeutic monoclonal antibodies (mAbs). Alteration in N-glycoforms may significantly modify the biological activity of mAbs. The unexpected and heterogeneous N-glycoforms are often reported, because it is affected by the culture medium, the efficiency of protein expression, and the physiological status of the host cells. Thus, accurate identification and quantification of their N-glycoform are necessary in order to control the production processes. In this study, IgG (Human serum), two NIST (National institute of standards and technology), and three unknown therapeutic mAb samples were analyzed by LC-MS/MS and GPA (GlycoProteome Analyzer) system1. As a result, the complex types of N-glycoforms were identified in IgG and unknown sample A, whereas different high-mannose and hybrid types of N-glycoforms were identified in two NIST samples and unknown sample B and C. The quantitative patterns of N-glycoform were similar between IgG and unknown sample A. The hybrid type and high-mannose type of N-glycoform were quantitatively increased in two NIST samples and unknown sample B and C, respectively. This analytical method will be useful for verification of safety and efficacy in various biopharmaceutical products such as therapeutic monoclonal antibodies.