The [3H]sugars were then separated into a number of monosaccharides and oligosaccharides by paper chromatography. Strong acid hydrolysis of two of the larger oligosaccharides released from the acceptor lipid followed by reduction with NaB3H4 gave [3H]mannitol and [3H]GlcN-ol in ratios of 22 and 32, indicating that these compounds probably were penta- and hexasaccharides. In addition, GlcNAc was shown to be at the reducing terminus and alpha-linked mannose at the nonreducing ends of the molecules. human milk oligosaccharides suggest that the acceptor lipid fraction is composed of oligosaccharides of (Man)n leads to GlcNAc leads to GlcNAc, probably attached to a polyprenol Structural basis for recognition of phosphorylated high mannose oligosaccharides by the cation-dependent mannose 6-phosphate receptor.Mannose 6-phosphate receptors (MPRs) play an important role in the targeting of newly synthesized soluble acid hydrolases to the lysosome in higher eukaryotic cells. These acid hydrolases carry mannose 6-phosphate recognition markers on their N-linked oligosaccharides that are recognized by two distinct MPRs the cation-dependent mannose 6-phosphate receptor and the insulin-like growth factor IIcation-independent mannose 6-phosphate receptor. Although much has been learned about the MPRs, it is unclear how these receptors interact with the highly diverse population of lysosomal enzymes. It is known that the terminal mannose 6-phosphate is essential for receptor binding. However, the results from several studies using synthetic oligosaccharides indicate that the binding site encompasses at least two sugars of the oligosaccharide. We now report the structure of the soluble extracytoplasmic domain of a glycosylation-deficient form of the bovine cation-dependent mannose 6-phosphate receptor complexed to pentamannosyl phosphate. Grab it today construct consists of the amino-terminal 154 amino acids (excluding the signal sequence) with glutamine substituted for asparagine at positions 31, 57, 68, and 87. The binding site of the receptor encompasses the phosphate group plus three of the five mannose rings of pentamannosyl phosphate. Receptor specificity for mannose arises from protein contacts with the 2-hydroxyl on the terminal mannose ring adjacent to the phosphate group. Glycosidic linkage preference originates from the minimization of unfavorable interactions between the ligand and receptor.Identification of plant polysaccharides by MALDI-TOF MS fingerprinting after periodate oxidation and thermal hydrolysis.Weilanden 9, 68 WG Wageningen, the Netherlands.Droevendaalsesteeg 1, 60 AA Wageningen, the Netherlands.Netherlands; Wageningen University & Research, Laboratory of Organic Chemistry, P.O. Box 26, 60 EG Wageningen, the Netherlands. An autoclave treatment at 121 °C on periodate-oxidized plant polysaccharides and mixes thereof was investigated for the release of oligosaccharides to obtain a generic polysaccharide depolymerization method for polysaccharides fingerprinting. Matrix-Assisted Laser Desorption Ionization Time-Of-Flight Mass Spectrometry (MALDI-TOF MS) analysis of the oligosaccharides released showed that each polysaccharide had a unique oligosaccharides profile, even the same type of polysaccharide derived from different sources andor having different fine structures (e.g. class of (arabino)xylans, galactomannans, glucans, or pectic materials). Various polysaccharide classes present in a polysaccharide mix could be identified based on significantly different (p 5) marker mz values present in the mass spectrum. Principal component analysis and hierarchical cluster analysis of the obtained MALDI-TOF MS data highlighted the structural heterogeneity of the polysaccharides studied, and clustered polysaccharide samples with resembling oligosaccharide profiles. Our approach represents a step further towards a generic and accessible identification of plant polysaccharides individually or in a mixture. Synthesis of sulfated oligosaccharides by cystic fibrosis trachea epithelial The mucin glycoproteins in tracheal mucus of patients with cystic fibrosis is more highly sulfated than the corresponding secretions from healthy individuals [16]. In order to further characterize these differences in sulfation and possibly also glycosylation patterns, we compared the structures of sulfated mucin oligosaccharides synthesized by continuously cultured human tracheal cells transformed by simian virus . The synthesis of highly sulfated oligosaccharide chains in mucins secreted by normal human epithelial and submucosal cell lines were compared with mucins formed by cystic fibrosis tracheal epithelial and submucosal cell lines.
human milk oligosaccharides|Grab it today
