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submitted on 07.06.2019 and posted on 07.06.2019by Edward Pallister, Matthew Choo, jien nee tai, Dawn leong, Wen-Qin Tang, Say-Kong Ng, Kun Huang, Andrea Marchesi, Peter Both, Chris Gray, Pauline Rudd, Sabine Flitsch, Terry Nguyen-Khuong
Sialic acids are cell surface sugars present in many animal
glycoproteins and are of particular interest in biopharmaceuticals, where lack of
sialylation can reduce bioactivity. Here we describe how α-2,6-sialyltransferase from Photobacterium Damselae can be used to markedly increase
sialylation of CHO produced alpha-1-antitrypsin. Detailed analysis of the
sialylation products showed that in addition to the expected α-2,6-sialylation of galactose, a second di-sialyl galactose
motif was produced, which had never been recorded on a mammalian glycoprotein. The
influence of this unique di-sialylation on the in vitro activity of alpha-1-antitrypsin was studied and a toolkit
of mass spectrometry methods to identify this new di-sialyl galactose motif in
complex mixtures was developed