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. 2020 Jul 9;59(37):16225–16232. doi: 10.1002/anie.202002147

Figure 6.

Figure 6

Glycation obscures differences between glycoform profiles of two Prolia® batches (old vs. new). Raw mass spectra of a) the intact and b) the de‐N‐glycosylated mAb, corresponding to 2 kDa‐sections of the respective zero‐charge spectra (the secondary x‐axes indicate the respective masses). c) Fractional glycoform abundances before and after correction for the effects of glycation. d) Inter‐batch differences of glycoform abundances as derived from (c). Lines connect points denoting identical glycoforms. The three most common glycoforms are labeled. pp: percentage points. e) Absolute deviations of observed/actual glycoform abundances from simulated abundances based on released N‐glycan data. In each batch, those five glycoforms are highlighted for which correction leads to the largest decrease in deviation (thick line: most pronounced decrease). Point areas are proportional to observed/actual glycoform abundance. Error bars represent (propagated) 95 % confidence intervals from five technical replicates. RMSD, root‐mean‐square deviation.