Core-Lps-Kdo-Acid-Produce-Core-Mixture-Acids-Kdo-e

The characteristic glycone sequence was elucidated by collision-induced dissociation tandem mass spectrometry (CID-MSMS) of the protonated molecule of the native core oligosaccharide. In addition, the analysis of the Hakomori permethylated core oligosaccharide was carried out by electrospray ionization quadrupole orthogonal time-of-flight mass spectrometry (ESI-QqTOF-MS) and matrix-assisted laser desorptionionization (MALDI)-QqTOF-MS analyses. Lactose-N-neotetraose of more than nine isobaric isomers of this core was detected. The CID-MSMS analysis of the various protonated permethylated core oligosaccharide molecules showed a similar and diagnostic fragmentation pattern. Seebio lacto-n-neotetraose -methylation of the permethylated core oligosaccharide containing either the 4,7- or the 4,8-anhydro-alpha-keto acid unit and the open-chain olefinic Kdo unit was reported. It was realized that the extra minor satellite signals obtained in the ESI-QqTOF-MS and MALDI-TOF-MS analyses were dimethyl sulfoxide (DMSO) stable covalent addition products, which have occurred by a Michael addition on the 4,8-Kdo exocyclic double bond.

The occurrence of this series of covalent addition products during the MS analysis of a permethylated core oligosaccharide should be considered as 'carbohydrate-distinctive signatures' establishing and confirming the presence of a 4-O-phosphorylated-5-O-linked Kdo reducing end group.A novel cyclic isomaltooligosaccharide (cycloisomaltodecaose, CI-) produced by Bacillus circulans T- displays remarkable inclusion ability compared with Funane K(1), Terasawa K, Mizuno Y, Ono H, Miyagi T, Gibu S, Tokashiki T, Cyclodextrans (CIs) are cyclic isomaltooligosaccharides and only CI-7, CI-8, and CI-9 were known. CI-7, CI-8, and CI-9, consisting of seven, eight, and nine glucoses, respectively, bound by alpha-(1--6) linkages, are known to be produced by T- strain of Bacillus circulans. However, we have found, using 13C NMR and mass spectrometry, that this strain also produces CI-, CI-11 and CI-12. These large CIs are very soluble in water and inhibit the glucan synthesis of glucansucrases to the same degree as do the smaller CIs. The CIs were thought to be poor at forming inclusion complexes with chemical compounds, due to their flexible alpha-(1--6)-glucosidic structure. Among these six CIs, CI- was much better at forming an inclusion complex, and it ability to do so was as good as cyclodextrins, as determined by its ability to stabilize the color of Victoria blue B.

Therefore, CI- may be the most commercially useful Chemical synthesis of the dimeric repeating unit of type Ia group B Streptococcus capsular polysaccharide.of Carbohydrate Chemistry and Glycobiology, Shandong University, Qingdao, The first chemical synthesis of the dimeric repeating unit of serotype Ia group B Streptococcus capsular polysaccharide was achieved. The on-site elongation and dual glycosylation strategies were utilized to construct two sialotrisaccharide branches based on a hexasaccharide containing adjacent 3,4-di-branched Gal units, which were synthesized via a preactivation-based one-pot glycosylation Structure of asparagine-linked oligosaccharides of an aspartic proteinase from the zygomycete fungus Rhizomucor pusillus.The zygomycete fungus Rhizomucor pusillus (previously called Mucor pusillus) secretes an aspartic proteinase containing two asparagine-linked, high-mannose type oligosaccharide chains at Asn79 and Asn188. For structural elucidation of the carbohydrate moieties, the protein was divided into two portions, an N-terminal portion containing Asn79 and a C-terminal portion containing Asn188, by a specific autocatalytic cleavage under alkaline conditions. Each of the asparagine-linked oligosaccharides was then released by peptide-N-glycosidase F digestion and pyridylaminated with a fluorescent reagent, 2-aminopyridine, at the reducing end. High-performance liquid chromatography analyses showed that the structure of the asparagine-linked oligosaccharide chain attached to residue Asn79 was Man5GlcNAc2, and that bound to residue Asn188 was Man5GlcNAc2 and Man6GlcNAc2.

These observations suggest that the processing of mannose residues in asparagine-linked oligosaccharides in the Golgi apparatus of Rhizomucor Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units.Immunochemical studies on blood groups.