Article
Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics.
Glycobiology - 1 May 2000
Raju T S, Briggs J B, Borge S M, Jones A J
Abstract excerpt
Immunoglobulins (IgG) are soluble serum glycoproteins in which the oligosaccharides play significant roles in the bioactivity and pharmacokinetics. Recombinant immuno-globulins (rIgG) produced in different host cells by recombinant DNA technology are becoming major therapeutic agents to treat life threatening diseases such as cancer. Since glycosylation is cell type specific, rIgGs produced in different host...
Topics
- Amidohydrolases
- Animals
- Carbohydrate Conformation
- Carbohydrate Sequence
- Galactose
- Genetic Variation
- Glycosylation
- Humans
- Hydrogen-Ion Concentration
- Immunoglobulin G
- Mannose
- Molecular Sequence Data
- N-Acetylneuraminic Acid