Notes

Model Vivo Carrageenin Infiltration Inflammatory Lesions
CST-II's recognition domain for acceptor substrates in α-(2→8)-sialylations.CST-II is a bacterial sialyltransferase known for its ability to perform α-(2→8)-sialylations using GM(3) related trisaccharide substrates. Previously, we probed the enzyme's substrate specificity and developed an efficient synthesis for α-(2→8)-oligosialosides, and we suggested that CST-II could have a very small substrate recognition domain. Here we report our full studies on CST-II's recognition feature for acceptor substrates. The current study further demonstrates the versatility of CST-II in preparing complex oligosaccharides that contain α-(2→8)-oligosialyl moieties.Ranking of gas-phase acidities and chloride affinities of monosaccharides and linkage specificity in collision-induced decompositions of negative ion electrospray-generated chloride adducts of oligosaccharides.

Negative ion electrospray-tandem mass spectrometry has been employed to study chloride adducts of saccharide molecules. Decompositions of [M + Cl]- obtained under identical low-energy collision conditions allow the approximate ranking of chloride affinities and gas-phase acidities of a series of isomeric monosaccharides. The ketohexoses are found to be more acidic than the aldohexoses. Seebio 2'-fucosyllactose adduct decompositions are examined for a glucopyranosyl fructose and a glucopyranosyl glucose series. For each disaccharide series, the linkage position is shown to markedly influence the favored pathways of [M + Cl]- decompositions, initiated either by loss of neutral HCl to form [M - H]- and possibly leading to further (consecutive) decompositions, or by loss of M to form Cl-. Upon formation of [M - H]-, both cross-ring cleavages and glycosidic bond decompositions were observed in varying degrees for the two series of disaccharides. Remarkably, for three non-reducing polysaccharides that each contain a terminal sucrose group at the downstream end, chlorine-containing product ions arising from cleavage of the Glcalpha-2Fru linkage have been observed.

Apart from Cl-, chlorine-containing product ions are not observed for any of the other disaccharides investigated, and they appear to be specifically diagnostic of a terminal Glcalpha-2Fru linkage. Their appearance is rationalized based upon a substantially reduced tendency for HCl loss from these non-reducing Anaphylaxis to galacto-oligosaccharides--an evaluation in an atopic population Soh JY(1)(2), Huang CH(1)(2), Chiang WC(3), Llanora GV(1), Lee AJ(1)(2), Loh University of Singapore, Singapore, Singapore.University of Singapore, Singapore, Singapore.Anaphylaxis to galacto-oligosaccharides (GOS), a prebiotic, has been described in atopic patients following its supplementation in commercial milk formula in South-East Asia. The epidemiology of this usual allergy to a carbohydrate is unknown. This study evaluated the prevalence of allergy to two formulations of commercial GOS, Vivinal™ GOS (vGOS) and Oligomate™ , in an atopic cohort. Atopic subjects (n = 487) from two specialist allergy clinics were surveyed via structured questionnaire and underwent skin prick tests to GOS.

Subjects with positive skin prick tests to GOS (n = , 6%) underwent basophil activation tests, and a subset (n = 13) underwent oral challenge tests to both formulations of GOS. Six subjects had positive challenges to vGOS; and none to Oligomate. By extrapolating the BAT and oral challenge results, the prevalence of allergy to vGOS is estimated at up to 3% (95% CI 2-5%) of our atopic population. Our findings show that GOS allergy may be common amongst atopics in Singapore.Transfer of two oligosaccharides to protein in a Chinese hamster ovary cell B211 which utilizes polyprenol for its N-linked glycosylation intermediates.B211, a glycosylation mutant isolated from Chinese hamster ovary cells, synthesizes - to 15-fold less Glc3Man9GlcNAc2-P-P-lipid, the substrate used by the oligosaccharide transferase in the synthesis of asparagine-linked glycoproteins. B211 cells are also - to 15-fold deficient in the glucosylation of oligosaccharide-lipid.

Despite these properties, protein glycosylation in B211 cells proceeds at a level similar to (% of) parental cells. We asked whether the near wild-type level of glycosylation was due to the transfer of alternative oligosaccharide structures to protein in B211 cells. The aberrant size of [35S]methionine-labeled VSV G protein and the increased percentage of endoglycosidase H-resistant tryptic peptides as compared to parental cells supported this hypothesis.
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