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- W2213049771 abstract "Most human plasma proteins are glycoproteins [1]. Oligosaccharides linked to proteins may contribute to receptor-mediated interactions, protein stability, clearance from circulation, and physiological function of the protein [2–4]. Human coagulation factors can be isolated from human plasma or produced recombinantly. Recombinant technology promises several major benefits for the production of human plasma proteins: the possibility of supplying purer proteins in quantity; little or no contamination with pathogenic materials; the possibility of creating modified coagulation factors with modified properties [5,6]. Given the importance of protein glycosylation for pharmacological activity, expression of such molecules in mammalian cells is therefore the one and only choice for manufacture of correctly glycosylated biopharmaceuticals [7,8]. Recently, we have described the recombinant expression, purification, and structural analysis of recombinant human coagulation factor IX (rh-FIX) [9,10]. Glycosylation analysis demonstrated that rh-FIX produced by transformed Chinese hamster ovary (CHO) cells exhibited complex-type glycosylation with carbohydrate chains capped with sialic acid α(2-3)-galactose groups. By contrast, human plasma-derived coagulation factor IX (hp-FIX) contained terminal sialic acid α(2-6)-galactose moities. In this article we describe the conversion of CHO cell-derived rh-FIX sialylation pattern into human-like sialylation patten in vitro. ©" @default.
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- W2213049771 date "1998-02-01" @default.
- W2213049771 modified "2023-10-18" @default.
- W2213049771 title "Recombinant Coagulation Factor IX" @default.
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- W2213049771 doi "https://doi.org/10.1016/s0049-3848(97)00303-4" @default.
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