Alteration in Glycosylation: Controlling the Diversity of Recombinant Glycoproteins

Autor:	Mary B. Sliwkowski, Thomas Ryll, George Dutina, Tina Etcheverry, Riley Speckart
Rok vydání:	1997
Předmět:	chemistry.chemical_classification Glycosylation Culture environment Chinese hamster ovary cell Disulfide bond law.invention Sialic acid carbohydrates (lipids) chemistry.chemical_compound chemistry Biochemistry law Recombinant DNA Glycoprotein
Zdroj:	Animal Cell Technology ISBN: 9789401062732
DOI:	10.1007/978-94-011-5404-8_101
Popis:	N-linked Oligosaccharides on a recombinant protein play a critical role in the metabolic behavior of the molecule. The extent of glycosylation on the protein can determine clearance rates and the ultimate pharmacokinctic profile. The amount of terminal sialylation is particularly important in this respect. Changes in the glyeosylation pattern due to changes in culture conditions will be shown for a model glyeoprotein produced in CHO cells. The parameter determining the sialic acid content will be discussed together with a method to control for this type of heterogeneity.
Databáze:	OpenAIRE
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