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Supplementary Figure 1 | Pharmaceutical Research

Supplementary Figure 1

From: Structural Characterisation of Non-Deamidated Acidic Variants of Erwinia chrysanthemi L-asparaginase Using Small-Angle X-ray Scattering and Ion-Mobility Mass Spectrometry

Supplementary Figure 1

Tandem MS/MS spectra of peptide unmodified peptide TGNGIVPPDEELPGLVSDSLNPAHAR (885.7868 m/z) [M+3H]3+ and deamidated peptide TGDGIVPPDEELPGLVSDSLNPAHAR (886.1136 m/z) [M+3H]3+. The abundant ions are highlighted. The mass shift of 1 Da for the b-series ions identified between unmodified and deamidated forms of the peptide, confirm the position of deamidation at N3. Also lack of mass shift in y-series ions identified also rules out deamidation and positions N21 and R26. Inset shows the isotope distribution of the parent ion. (GIF 182 kb)

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