Table of contents:
I. Introduction ... I.1. General definitions... I.2. Glycosylation of proteins ... I.2.1. Introduction to glycosylation ... I.2.2. Structure and biosynthesis of the N-glycans ... I.3. Therapeutic glycoproteins ... I.3.1. Therapeutic mAbs ... I.3.1.1. Structure of therapeutic mAbs ... I.3.1.2. Mechanisms of action of therapeutic mAbs ... I.3.2. Antibody drug conjugates ... I.3.3. Fc-fusion proteins ... I.3.4. Therapeutic enzymes ... I.3.5. Therapeutic hormones ... I.3.6. Therapeutic cytokines ... I.3.7. Therapeutic clotting factors ... I.4. Advantages and disadvantages of therapeutic proteins ... I.5. Production of therapeutic glycoproteins ... I.5.1. Recombinant DNA technology ...
I.5.2. Modulation of glycosylation during the production of
IV.1. LC-MS analysis combined with Principal Component Analysis and Soft Independent Modelling by Class Analogy for a better detection of changes in N-glycosylation profiles of therapeutic glycoproteins ... IV.1.1. Introduction ... IV.1.2. Results and Discussion ... IV.1.3. Conclusion ... IV.2. Batch-to-batch N-glycosylation Study of Infliximab, Trastuzumab, and Bevacizumab, and Stability Study of Bevacizumab ...
IV.2.1. Introduction ... IV.2.2. Results and Discussion ... IV.2.3. Conclusion ... IV.3. Rapid N-glycans profiling by LC-MS using free labeled approach and online solid phase extraction (article in preparation). ...
