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This article reviews structure-activity relationship (SAR) of structurally-defined Alginate oligosaccharide protects against enterotoxigenic Escherichia coli-induced porcine intestinal barrier injury.Alginate oligosaccharide (AOS) possesses various pharmaceutical benefits, making it an attractive candidate for biomedical applications. In the present study, we prepared AOS by depolymerising alginate; its degree of polymerisation mainly ranged from 2 to 8. We confirmed the enteroprotective potential of AOS against enterotoxigenic Escherichia coli (ETEC)-induced intestinal barrier injury in weaned pigs. Next, [https://en.wikipedia.org/wiki/Lacto-N-tetraose Seebio lacto-n-neotetraose] illustrated the mechanisms underlying this effect of AOS using the porcine small intestinal epithelial cell line IPEC-J2. AOS potently reduced the binding of the bacteria-deprived endotoxin lipopolysaccharide (LPS) to the IPEC-J2 cell surface.<br /><br /> Moreover, it suppressed the LPS-induced production of pro-inflammatory cytokines and the nuclear translocation of nuclear factor-κB intestinal epithelium from ETEC-induced inflammatory injury by preventing the activation of NF-κB, implying that AOS could be used as an anti-inflammatory agent for treating inflammation-related intestinal diseases in mammals.[Characteristics of the fermentation of maltose, sucrose, lactose and raffinose by barotolerant bacteria at elevated hydrostatic pressures].The role of certain sugars in the production of capsular polysaccharide and lactic acid by Streptococcus pyogenes.Formation of ethyl ferulate from feruloylated oligosaccharide by transesterification of rice koji enzyme under sake mash conditions.Nakano Shimoshinjyo, Akita195, Japan.Formation of ethyl ferulate (EF) and ferulic acid (FA) under sake mash conditions was studied using feruloylated oligosaccharide (FO), prepared from rice grains, as the substrate for rice koji enzyme. EF and FA were produced from FO over six times faster than from alkyl ferulates however, under the same ethanol concentration, only small differences were observed between the EFFA ratios when either FO or methyl ferulate were used as substrates.<br /><br /> Esterification and hydrolysis of FO or methyl ferulate showed similar pH dependencies and similar EFFA ratios for each substrate in all of the pH ranges tested. Ethanol concentration clearly affected the EFFA ratio; the ratio increased as ethanol concentration increased. Formation of EF and FA in the sake mash simulated rice digest was accelerated by addition of exogenous FO. These results indicated that supply of FO to sake mash is a crucial step for EF and FA formation, and ethanol is an influencing factor in the EFFA ratio. [http://www.allinno.com/product/healthcare/674.html Oligosaccharides] suggested that EF and FA are formed through a common feruloylated enzyme intermediate complex by transesterification or hydrolysis, and these reactions Intracellular forms of transferrin oligosaccharide chains in rat liver.Glycosylation of transferrin was investigated in vivo by using antibody monospecific for rat serum transferrin. Pulse-chase experiments indicated that, after intravenous injection of [35S]methionine, labeled transferrin appeared in the rough and smooth microsomes and Golgi subfractions in rapid succession in min and that an additional min was required for it to be secreted.<br /><br /> Most of the intracellular transferrin (95%) immunoprecipitated from the total microsome fraction was sensitive to endo-beta-N-acetylglucosaminidase H (endo H), whereas serum transferrin was completely resistant to it. Further fractionation of the total microsomes has revealed that the intracellular transferrin immunoprecipitated from the rough and smooth microsomes and GF3 are all endo-H-sensitive and most of the endo-H-sensitive oligosaccharides were eluted at the position corresponding to Man8GlcNAc on high-resolution Bio-Gel chromatography. This finding suggests that the major form of intracellular transferrin oligosaccharide in the course of intracellular transport from the endoplasmic reticulum to the Golgi apparatus is Man8GlcNAc2. Endo-H-resistant forms were first detected in the GF2 but more in GF1, most of which were sensitive to neuraminidase. Since the heavy Golgi subfraction contains mainly cis-Golgi elements, such as cisternae, and the light subfraction mainly trans-Golgi elements, such as secretory granules, it is strongly suggested that the processing of these large mannosyloligosaccharide chains and the subsequent addition of terminal sugars to them are performed successively in the trans-Golgi region just before secretion.DOI 111j432-33983.t7736.<br /><br />xBiosynthesis of the oligosaccharides of influenza viral glycoproteins.