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The analysis and modification of glycans of recombinant proteins continues to be active and challenging area of research and for the successful manufacture of these proteins. In Cell Engineering, volume3:Glycosylation, Dr. Mohammed Al-Rubeai has compiled a group of articles that will provide research workers not only with reviews of the advances that have been made in all facets of the subject but with an in-depth assessment of the state of the art methodology and the various approaches for the improvement of glycoprotein production. Particularly important in this respect is the advances made in the development of genetically engineered host cell lines with novel glycosylation properties, as well as the integration of mass spectrophotometric analysis with separation techniques.
This volume is intended not only for research students and senior scientists in cell culture and glycobiology, but also for industrial biotechnologists and biochemical engineers interested in the production of therapeutic glycoproteins, virus vector and ex vivo expansion of human cells for medical treatment.
Content Level »Research
Keywords »Mammalia - Vivo - development - glycoprotein - protein - proteins
1. Analysis of Glycans of Recombinant Glycoproteins; T. Merry, et al.
2. The Effect of Cell Culture Parameters on Protein Glycosylation; V. Restelli, M. Butler.
3. Glycosylation of Recombinant IgG Antibodies and its Relevance for Therapeutic Applications; R. Jefferis.
4. Cellular Modification for the Improvement of the Glycosylation Pathway; L. Krummen, S. Weikert.
5. Controlling Carbohydrates on Recombinant Glycoproteins; N. Jenkins, et al.
6. Targeting of Genetically Engineered Glycosyltransferases to in Vivo Functional Golgi Subcompartments of Mammalian Cells; E. Grabenhorst, et al.
7. A Metabolic Substrate-Based Approach to Engineering New Chemical Reactivity into Cellular Sialoglycoconjugates; K.J. Yarema.
8. Addressing Insect Cell Glycosylation Deficiencies Through Metabolic Engineering; S.M. Lawrence, M.J. Betenbaugh.
9. Asparagine-Linked Glycosylational Modifications in Yeast; J.-M. Wu, et al.