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• W2920646543 abstract "ABSTRACT Human Factor IX is a highly post-translationally modified protein that is an important clotting factor in the blood coagulation cascade. Functional deficiencies in Factor IX result in the bleeding disorder haemophilia B, which is treated with plasma-derived or recombinant Factor IX concentrates. Here, we investigated the post-translational modifications of human serum-derived Factor IX and report previously undescribed O -linked monosaccharide compositions at serine 141 and a novel site of glycosylation. At serine 141 we observed two monosaccharide compositions, with HexNAc 1 Hex 1 NeuAc 2 dominant and a low level of HexNAc 1 Hex 1 NeuAc 1 . This O -linked site lies N-terminal to the first cleavage site for the activation peptide, an important region of the protein that is removed to activate Factor IX. The novel site is an N -linked site in the serine protease domain with low occupancy in a non-canonical consensus motif at asparagine 258, observed with a HexNAc 4 Hex 5 NeuAc 2 monosaccharide composition attached. This is the first reported instance of a site of modification in the serine protease domain. The description of these glycosylation events provides a basis for future functional studies and contributes to structural characterisation of native Factor IX for the production of effective therapeutic biosimilars and biobetters." @default.
• W2920646543 created "2019-03-11" @default.
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• W2920646543 date "2019-03-05" @default.
• W2920646543 modified "2023-10-16" @default.
• W2920646543 title "Identification of novel glycosylation events on human serum-derived Factor IX" @default.
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• W2920646543 doi "https://doi.org/10.1101/567941" @default.
• W2920646543 hasPublicationYear "2019" @default.
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