Abstract:In order to study the effect of glycosylation on its biological activities, and to develop TNFalpha with less deleterious effects, recombinant human TNFalpha was chemically coupled with N-acetylneuraminic acid (NeuAc). NeuAc with C9 spacer was coupled to TNFalpha by acyl azide method. Two glycosylated TNFalphas, designated L NeuAc-TNFalpha and H NeuAc-TNFalpha, were purified by anion-exchange chromatography. NeuAc coupling to TNFalpha was confirmed by lectin blotting. Average number of carbohydrate molecules i… Show more
“…This type of in vitro glycosylation is suggested to be applicable to other glycoproteins containing terminal N ‐acetylglucosamine and galactose residues and could prove to be useful in increasing the serum half‐life and homogeneity of therapeutic glycoproteins. Recently, Hayashi et al66 reported the chemical sialylation of TNF‐alpha using an acyl azide method and proofed that also chemical methods can be used to sialylated glycoproteins.…”
Section: Increasing Sialylation Of Recombinant Glycoproteinsmentioning
“…This type of in vitro glycosylation is suggested to be applicable to other glycoproteins containing terminal N ‐acetylglucosamine and galactose residues and could prove to be useful in increasing the serum half‐life and homogeneity of therapeutic glycoproteins. Recently, Hayashi et al66 reported the chemical sialylation of TNF‐alpha using an acyl azide method and proofed that also chemical methods can be used to sialylated glycoproteins.…”
Section: Increasing Sialylation Of Recombinant Glycoproteinsmentioning
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