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Structurally, they represent a highly complex class of analyte, where the main core oligosaccharide structures are built from galactose and N-acetylglucosamine, linked by 1-3 or 1-4 glycosidic linkages and potentially modified with fucose and sialic acid residues. [http://extension.unimagdalena.edu.co/extension/Lists/Contactenos/DispForm.aspx?ID=981055 Get it now] can be linear or branched. Additional structural complexity in samples can be induced by endogenous exoglycosidase activity or chemical procedures during the sample preparation. Here, we show that using matrix-assisted laser desorptionionization (MALDI) quadrupole-time-of-flight (Q-TOF) collision-induced dissociation (CID) as a fast screening method, diagnostic structural information about single oligosaccharide components present in a complex mixture can be obtained. According to sequencing data on 14 out of 22 parent ions detected in a single high molecular weight oligosaccharide chromatographic fraction, different oligosaccharide structure types, corresponding to over isomeric oligosaccharide structures and over 0 possible HMO isomers when biosynthetic linkage variations were taken into account, were postulated. For MSMS data analysis, we used the de novo sequencing approach using diagnostic ion analysis on reduced oligosaccharides by following known biosynthetic rules.<br /><br /> Using this approach, de novo characterization has been achieved also for the structures, which could not have Fractionation of sialyl oligosaccharides of human milk by ion-exchange Immunomodulatory effects of breast milk oligosaccharides.Breast milk oligosaccharides are excreted in urine in amounts that suggest that they may exist in the circulation at levels compatible with a physiological function. Some oligosaccharides have structural similarity to cellular adhesion molecules and may influence adhesion of cells in breast fed infants. In this study, breast milk oligosaccharides were purified and incubated in assays of cell adhesion. They were found to inhibit neutrophil adhesion to stimulated vascular endothelial cells in a dose dependent fashion. In contrast they enhanced platelet-neutrophil complex formation. These results indicate that breast milk oligosaccharides may play a physiological role in modulating Occurrence of oligosaccharides in feces of breast-fed babies in their first six months of life and the corresponding breast milk.<br /><br />The characterization of oligosaccharides in the feces of breast-fed babies is a valuable tool for monitoring the gastrointestinal fate of human milk oligosaccharides (HMOs). In the present study we monitored fecal oligosaccharide profiles together with the HMO-profiles of the respective breast milks up to six months postpartum, by means of capillary electrophoresis-laser induced fluorescence detection and mass spectrometry. Eleven motherchild pairs were included. [https://milkyway.cs.rpi.edu/milkyway/show_user.php?userid=6398889 Human Milk Glycans] - and Lewis-type included all combinations [Le(a-b+), Le(a+b-), Le(a-b-)]. The fecal HMO-profiles in the first few months of life are either predominantly composed of neutral or acidic HMOs and are possibly effected by the HMO-fingerprint in the respective breast milk. Independent of the initial presence of acidic or neutral fecal HMOs, a gradual change to blood-group specific oligosaccharides was observed. Their presence pointed to a gastrointestinal degradation of the feeding-related HMOs, followed by conjugation with blood group specific antigenic determinants present in the gastrointestinal mucus layer.<br /><br /> Eleven of these 'hybrid'-oligosaccharides were annotated in this study. When solid food was introduced, no HMOs and their degradation- and metabolization products were recovered in the fecal samples.Oligosaccharides of human milk isolation and characterization of two new nonasaccharides, monofucosyllacto-N-octaose and monofucosyllacto-N-neooctaose.Differentiation of 'isobaric' peptides and human milk oligosaccharides by exact mass measurements using electrospray ionization orthogonal time-of-flight Exact mass determination is performed by electrospray ionization orthogonal time-of-flight mass analysis. For peptides in the mass range of 10-10 Da a mass error of 5 ppm is achieved with internal calibration within a single mass measurement provided peak intensities are high. Peptides containing isobaric amino acids like glutamine and lysine can thus be easily differentiated by their mass. In cases where more than one of these isobaric amino acids are present, the position of the amino acid can be revealed by exactly determining the mass differences between adjacent Yi fragment ions in the collision-induced dissociation spectrum.