Fig. 2
From: The glycosylation design space for recombinant lysosomal replacement enzymes produced in CHO cells
Site-specific glycan analyses of selected α-galactosidase A (GLA) glycoforms produced in the initial knockout/knock-in (KO/KI) CHO cell screen. a The two most abundant glycan structures at N-glycosites (N108, N161, and N184) of GLA produced in CHO wild type (WT) are shown, and in b–t the two most abundant glycans for GLA produced in engineered CHO clones are shown as indicated. The detailed N-glycan analyses of all GLA glycoforms are shown in Supplementary Fig. 2 together with additional variants. Each glycan structure was confirmed by targeted tandem mass spectrometry (MS/MS) analysis (Supplementary Fig. 5). Details regarding the stacking ancestry and sequence analysis are shown in Supplementary Table 2 and Supplementary Data 1
