.. For sequence and configuration elucidation of Ki16425 mouse sialylated structures, the released oligosaccharides of human synovial lubricin were incubated with sialidase S (Streptococcus pneumonia) specific for α2-3 linked sialic acid. After 16 h incubation, a complete degradation of the [M - H]- ions at m/z 1040 (NeuAc1Hex2HexNAc1HexNAcol) and [M - H]- ions at m/z 1331 Inhibitors,research,lifescience,medical (NeuAc2Hex2HexNAc1HexNAcol) (Figure 2b) could be shown, accompanied with an increase in the intensity of the [M - H]- ions at m/z 749 (Hex2HexNAc1HexNAcol (Figure 2b), indicated that this was the exoglycosidase product generated after removal of sialic
Inhibitors,research,lifescience,medical acid from
the substrate. The MS2 spectral intensity correlation analysis of the [M - H]- ions at m/z 749 with spectra reported in the MS2 database UniCarb-DB suggests that this was a core 2 structure with Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAc configuration (Table 1) which can be terminated with one sialic acid (on either of the branches) and with two sialic acid Inhibitors,research,lifescience,medical (on both branches). The complete degradation of the [M - H]- ions at m/z 1331 and m/z 1040 indicated that the NeuAc moiety in both the structures are α2-3 linked (Figure 2b) and the MS2 spectral intensity correlation analysis of the structure created after the treatment (i.e [M - H]- ions at m/z 749) further extended the assignment of the structure to be Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcol (Table 1). The intensity of the product (i.e only 46%) did not increase proportionally to the decrease
of the Inhibitors,research,lifescience,medical substrates due to differences in ionization efficiency. The complete degradation of the sialylated core 1 with [M - H]- ions at m/z 675 (NeuAc1Hex1HexNAcol) could also be observed. This indicated that the NeuAc moiety is α2-3 linked to the Galβ1-3GalNAc α1-Ser/Thr sequence of the core 1 structure when the MS2 spectra of the structure ([M Inhibitors,research,lifescience,medical - H]- ions at m/z 384) created after the treatment were compared with spectra reported Phosphoprotein phosphatase in the MS2 database UniCarb-DB (Table 1). 2.2. Identification of 4 Linked Terminal GlcNAc Moiety in Porcine Gastric Mucins (PGM) The exoglycosidase digestion will always be restricted to the availability of specific exoglycosidases. We identified structures in porcine gastric mucin (PGM) oligosaccharides with terminal HexNAc that was not affected by various hexosaminidases [22] (Figure 3), including β- N-acetylhexosaminidase from jack bean (JBH, removes both β-linked GlcNAc and GalNAc). We wanted to investigate whether we could further characterize the nature of this terminal HexNAc by LC-MS2 and LC-MS3.
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