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PubMed1995

Effects of the lipid-saccharide complex and unsaponifiable matter from sunflowers on liver lipid metabolism and intestinal flora in rats.

The effects of the flower lipid-saccharide complex and unsaponifiable matter (1 g/kg of diet) from the sunflower on liver lipid metabolism and intestinal flora was studied in rats given cholesterol-enriched diets. After six weeks of feeding, the microsomal cholesterol concentration in the liver had been significantly reduced with the sunflower diet. The ratio of cholesterol/phospholipid was also reduced by the sunflower diet. The 3-hydroxy-3-methylglutaryl coenzyme A reductase activity of the sunflower groups was significantly lower than that of the control group. There was no significant difference in the cholesterol 7 alpha-hydroxylase activity, although this tended to increase with dietary sunflower consumption. The number of Bacillus in the cecum flora was significantly higher in the lipid-saccharide complex group than in the other groups, while Bifidobacterium and Eubacterium in the cecum flora was significantly higher in the unsaponifiable matter group when compared to the control group. These results suggest that the lipid-saccharide complex and unsaponifiable matter in the sunflower are related to liver cholesterol synthesis and intestinal flora.

Animal Nutritional Physiological Phenomena↗
PubMed1989

Aversiveness of denatonium saccharide and quinine in grasshopper mice Onychomys leukogaster.

The responses toward denatonium saccharide and quinine by three rodent species differ from those exhibited by humans. This study measured the relative aversiveness of these two compounds in grasshopper mice (Onychomys leucogaster) to determine if this species responded similarly to or differently from these other rodents. In a choice test, the mice clearly preferred quinine over denatonium saccharide at concentrations of 1/10,000 and 1/50,000, but only marginally preferred quinine at a concentration of 1/1000. When denatonium or quinine was paired with toxicosis, both suppressed drinking at concentrations from 1/10,000 to 1/50,000, but only denatonium suppressed drinking at 1/100,000. Neither compound suppressed drinking at 1 part in million. Grasshopper mice perceived denatonium saccharide as more aversive than quinine in both experiments. Such a response resembled the behavior of humans more than that of the other three rodents previously tested.

Animals↗
PubMed1998

Saccharide-binding properties of boar AQN spermadhesins and DQH sperm surface protein.

Heparin-binding proteins BHB 2-BHB 5 were purified from boar seminal plasma by affinity chromatography on a heparin-polyacrylamide column and reversed phase HPLC. Three of the proteins, BHB 3-BHB 5, were found to be identical to spermadhesins AQN 1-AQN 3 isolated from boar spermatozoa. The lectin-like properties of the isolated proteins BHB 2-BHB 5 were studied using double-diffusion in agarose gel, enzyme-linked binding assay, and inhibition assays of erythroagglutinating activity. It was found that proteins BHB 3-BHB 5 (spermadhesins AQN 1-AQN 3) interacted with glycoproteins containing O-glycosidically bound oligosaccharide chains, but not with those containing only N-linked carbohydrate chains. The strongest interaction was observed between BHB 3 (AQN 1) and desialyzed bovine submaxillary gland mucin, the glycoprotein containing only O-glycosidically linked saccharides. No interaction of BHB 3-BHB 5 proteins with simple saccharides, their derivatives or acidic polysaccharides was observed. Both the hemagglutinating activity and saccharide-binding properties of BHB 2 protein were quite different. Agglutinating activity of human erythrocytes by BHB 2 protein was significantly higher than that by BHB 3-BHB 5 proteins (AQN spermadhesins). In contrast to AQN spermadhesins, BHB 2 protein (DQH sperm surface protein) interacted strongly with acidic polysaccharides and sialyzed glycoproteins, but no binding of desialyzed glycoproteins as well as N-acetyl-alpha-D-galactosaminyl-O-serine,simple monosaccharides and amino sugars was observed.

Animals↗
PubMed2000

Characterization of saccharide-CRM197 conjugate vaccines.

A seven-valent pneumococcal conjugate and a Group C Meningococcal conjugate are at the late stage of development. Clinical studies have demonstrated the efficacy and safety of these vaccines and licensure of these vaccines will be approved in the near future. Several new techniques have been proposed for characterizing polysaccharide-protein conjugates and their production intermediates. We are evaluating some of these new techniques, particularly NMR and MALLS, to determine whether or not they provide useful information for conjugate production. In the production of polysaccharide protein conjugates, the degree of saccharide activation, location of activation site, and the molecular weight of activated saccharides may typically be determined. In our evaluation, techniques such as NMR and MALLS may have a limited applicability for testing polysaccharides and activated saccharides.

Animals↗
PubMed2003

[Effect of saccharides in the teicoplanin stationary phase on the separation of enantiomers of the phenylcarbamic type using HPLC].

The paper presents the results obtained with the use of two chiral stationary phases (CSP) based on a macromolecular antibiotic agent--teikoplanin containing saccharide parts (CHIROBIOTIC T) and teikoplanin without saccharide parts (CHIROBIOTIC TAG). Racemic mixtures of 1-methyl-2-piperidinoethyl esters of 2-, 3-, and 4-alkoxyphenylcarbamic acids were examined. The investigation included interactions between separated substances and CSP, and the effect of separation of the enantiomers under study on the value of the differentiation factor (Rij) under identical chromatographic conditions with the use of the method of high-performance liquid chromatography (HPLC). On the basis of the obtained results, it is possible to report that CSP-CHIROBIOTIC TAG is more advantageous for the substances of the type of 1-methyl-2-piperidinoethyl esters of 2-, 3-, and 4-alkoxyphenylcarbamic acids, because it does not contain a saccharide part, which decreases the possibility of non-polar interactions which exert a negative effect on the Rij value.

Anti-Bacterial Agents↗
PubMed2003

[Saccharide analysis of si-wu-tang by automated multiple development and off-line coupling thin layer chromatography electrospray ionization mass spectrometry techniques].

OBJECTIVE: To make qualitative analysis on saccharide spots in thin layer chromatography (TLC) chromatogram of SI-WU-TANG extract C, which possesses blood-enrichment activity. METHOD: TLC chromatogram of SI-WU-TANG extract C was obtained by using Automated Multiple Development (AMD) method. 4 major spots in the chromatogram were analyzed by off-line coupling TLC electrospray ionization mass spectrometry (ESI-MS) technique. Moreover, composition of monosaccharides in the fraction was analyzed by AMD technique. RESULT: Main constituents of substances from the 4 spots were monosaccharide, disaccharide, trisaccharide and tetrasaccharide respectively. Monosaccharide was mainly composed of fructose and glucose. CONCLUSION: Off-line coupling TLC ESI-MS can simply and rapidly provide qualitative examination of saccharide spots in TLC chromatogram of Traditional Chinese Medicine. AMD method can make good separation of 8 frequently-observed monosaccharides in a regular 10 cm silica gel plate, the process of which was automated, AMD and off-line coupling TLC ESI-MS techniques show good value in saccharides analysis.

Angelica sinensis↗
PubMed1985

Biosynthesis of sulfated saccharides N-glycosidically linked to the protein via glucose. Purification and identification of sulfated dolichyl monophosphoryl tetrasaccharides from halobacteria.

A novel type of N-glycosidic linkage, asparaginyl glucose, occurs in the cell surface glycoprotein of halobacteria (Wieland, F., Heitzer, R., and Schaefer, W. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 5470-5474). Sulfated oligosaccharides containing glucuronic acids are attached to the polypeptide chain via this linkage. Here we describe the isolation and chemical characterization of lipid-linked precursors of these saccharides, and these have the following new features. Rather than the bacterial undecaprenol, a C60-dolichol is the carrier lipid. The oligosaccharide is bound to this lipid via a monophosphate, rather than a pyrophosphate bridge. Sulfation of the saccharides is completed while they are linked to lipid and does not occur after transfer of the saccharides to protein.

Asparagine↗
PubMed1996

Relationship between kinetic properties of gamma-glutamyl transpeptidase and the structure of its saccharide moiety.

Gamma-glutamyl transpeptidase (EC 2.3.2.2; GGT) is a plasma-membrane bound glycoenzyme, the saccharide moiety of which is rather heterogeneous and organ specific. It has been stated that GGT catalyses three types of reactions, i.e., hydrolysis, transpeptidation and autotranspeptidation. The initial velocity equation, involving all these reactions, is shown in the present report. Mathematical analysis of the equation resulting in a definition of the constant of half saturation (Khs). The value of Khs was used for characterization of kinetics of GGT from rat organs differing in the structure of GGT oligosaccharide chains. No significant organ differences were found, when the Khs values of GGT from the brain, kidney and pancreas equalled 0.61 mM, 0.68 mM and 0.68, respectively. On the contrary, when two different glycoforms of GGT from the pancreas were compared, distinct values of Khs were obtained (1.43 mM and 0.67 mM, respectively). It is therefore being suggested that the saccharide chains of GGT are involved in its kinetic properties. However, this effect is masked when the enzyme, non-fractionated into glycoforms, is analysed, even though the saccharide moiety is specific for the organ studied.

Animals↗
PubMed1976

Lipid-saccharide intermediates in glycoprotein biosynthesis. III. Comparison of oligosaccharide-lipids formed by slices from several tissues.

The synthesis of oligosaccharide-lipids thought to play a role in the attachment of carbohydrate to protein has been studied in incubations of slices from calf kidney, pancreas, thymus, and liver, as well as from hen oviduct. These compounds were characterized after radiolabeling of their saccharide moiety by incubation with [14C]glucose or [14C]mannose and a comparison was made with the oligosaccharide-lipid produced by thyroid slices. Furthermore, the unlabeled glycolipid was prepared from hen oviduct for the purpose of quantitating its sugar constituents. Purification of the oligosaccharide-lipids extracted with chloroform/methanol/water (10/10/3) was achieved by DEAE-cellulose chromatography and their carbohydrate moieties were released by mild acid hydrolysis. On the basis of gel filtration it was determined that the lipid-bound oligosaccharides formed by oviduct, thymus, kidney, and liver had molecular weights comparable to that from thyroid (about 2400). The saccharide moiety of the glycolipid from pancreas was however distinctly smaller in size with a molecular weight of approximately 1800. Analyses of the radiolabeled oligosaccharide-lipids from oviduct, kidney, and thymus indicated that they, like the compound from thyroid slices, but unlike those believed to be formed by cell-free systems from various tissues, contained glucose in addition to mannose and N-acetylglucosamine as their monosaccharide constituents. This compositional data was supported by the finding that the unlabeled oligosaccharide from oviduct consists of 10 mannose, 1 glucose, and 2 N-acetylglucosamine residues. Sodium borohydride reduction of this oviduct saccharide moiety indicated that 1 of the 2 glucosamines was situated in a reducing terminal position. The radiolabeled oligosaccharide from the glycolipid produced by pancreas differed from the others analyzed in that it contained only trace amounts of glucose. Upon treatment with alpha-mannosidase this glucose-deficient pancreatic oligosaccharide was extensively digested (85% of the mannose released). In contrast, the carbohydrate moieties of oviduct, kidney, and thymus, like that of thyroid, underwent a more limited digestion with the alpha-mannosidase (55% or less of the mannose released) suggesting that the presence of glucose may serve to block a more complete degradation of these oligosaccharides by this enzyme.

Acetylglucosamine↗
PubMedDate not supplied

Determination of saccharides labelled with a fluorescent reagent, DBD-ProCZ, by liquid chromatography.

Saccharides were determined by high-performance liquid chromatography (HPLC) after precolumn tagging with 4-(2-carbazoylpyrrolidin-1-yl)-7-(N,N-dimethylaminosulphonyl )-2,1, 3-benzoxadiazole (DBD-ProCZ). The tagging conditions were optimized with D-glucose. Monosaccharides and oligosaccharides were efficiently labelled under conditions of 65 degrees C for 180 min in water: acetonitrile mixture containing 0.5% trichloroacetic acid (TCA). The resulting derivatives were detected at 540 nm (excitation at 450 nm) after separation by HPLC. The separation of individual saccharides was possible using water: acetonitrile as the mobile phase using a reversed-phase column (Inertsil ODS-80A) and a normal-phase column (TSKgel Amide-80). N-Acetyl-D-glucosamine (GluNAC), N-acetyllactosamine (LacNAC) and tri-N-acetyl-chitotriose (tri-N-AceChito), which are components of glycoconjugates, were completely separated with an isocratic elution using as Inertsil ODS column. The on-column detection limit with the proposed HPLC separation and fluorescence detection at the low pmol level.

Chromatography, High Pressure Liquid↗
PubMed1989

The structure of the saccharide-binding site of concanavalin A.

A complex of concanavalin A with methyl alpha-D-mannopyranoside has been crystallized in space group P212121 with a = 123.9 A, b = 129.1 A and c = 67.5 A. X-ray diffraction intensities to 2.9 A resolution have been collected on a Xentronics/Nicolet area detector. The structure has been solved by molecular replacement where the starting model was based on refined coordinates of an I222 crystal of saccharide-free concanavalin A. The structure of the saccharide complex was refined by restrained least-squares methods to an R-factor value of 0.19. In this crystal form, the asymmetric unit contains four protein subunits, to each of which a molecule of mannoside is bound in a shallow crevice near the surface of the protein. The methyl alpha-D-mannopyranoside molecule is bound in the C1 chair conformation 8.7 A from the calcium-binding site and 12.8 A from the transition metal-binding site. A network of seven hydrogen bonds connects oxygen atoms O-3, O-4, O-5 and O-6 of the mannoside to residues Asn14, Leu99, Tyr100, Asp208 and Arg228. O-2 and O-1 of the mannoside extend into the solvent. O-2 is hydrogen-bonded through a water molecule to an adjacent asymmetric unit. O-1 is not involved in any hydrogen bond and there is no fixed position for its methyl substituent.

Binding Sites↗
PubMedDate not supplied

Studies of the binding activity of phage G13 to synthetic trisaccharides analogous to binding structures in Salmonella typhimurium and Escherichia coli C core saccharide. Correlation between conformation and binding activity.

Phage G13 binds to the carbohydrate part of lipopolysaccharides from rough mutants of Salmonella and Escherichia coli as the first event of infection. Equilibrium dialysis inhibition studies with native and synthetic trisaccharides as inhibitors suggested that phage G13 recognizes branched oligosaccharides having 6-O-alpha- or 7-O-alpha-glycosyl groups with alpha-Man(1----3) [alpha-Man(1----6)]Man (Man[Man]Man) and alpha-Glc(1----3)-[alpha-Hep(1----7)] alpha-Hep(1----3) alpha-Hep(1----5)Kdo as the smallest saccharides with inhibitory activity (Wollin et al., 1989). Of four synthetic analogues to Man[Man]Man only Man(1----3)[alpha-Gal(1----6)]alpha-Man-OMe (Man[Gal]-Man) and alpha-Glc(1----3)[alpha-Hep(1----7)]alpha-Hep-OMe (Glc[Hep]Hep) inhibited the binding of labelled E. coli C core nonasaccharide ligand to G13 with activities which were 10- and 15-fold lower than Man[Man]Man. The trisaccharides alpha-Man(1----3)[alpha-Glc(1----6)[alpha-Man-OMe (Man[Glc]Mann) and alpha-Man(1---3)[alpha-Tal(1----6)]alpha-Man-OMe (Man[Tal]Man) showed no inhibition at concentrations 75-fold higher than Man[Man]Man. Minimum energy conformation calculations of the saccharides using the GESA method showed that the 6-O-alpha-Man group in Man[Man]Man and the 7-O-alpha-Hep group SL805 pentasaccharide expose their OH-2 and OH-3 groups in a similar way and these are postulated to be key structural features for binding activity. The importance of hydroxy groups at certain positions is implied from the fact that both manno- and galacto-isomers are active. We also conclude that the O6-C6-C5-O5-C1 region of the 3-O-alpha-glycosyl group in the Man[Man]Man trisaccharide, or part of it, is important for the G13 binding activity.

Bacteriophages↗
PubMedDate not supplied

Specific hemoglobin (poly)saccharide recognition.

Hemoglobin (Hb) is not a glycoprotein but can easily be glycosylated by a non-enzymatic mechanism. Based on some kinetic particularities, consisting in a faster glycosylation of the amine terminal group of the beta-chain located on the allosteric site, a hypothesis of a recognition center for specific sugars has been advanced. Affinity chromatography materials based on epichlorohydrin crosslinked amylose, agarose and dextran (Sephadex), were used. A specific interaction with the CL-amylose (alpha-1,4-glycosidic links) was found, while for Sephadex (alpha-1,6-glycosidic links), no Hb retention was observed. An affinity retention of hemoglobins (human and bovine) on agarose (a galactose containing carbohydrate) has also been established. Chromatographic studies of Hb competitive elution with several monosaccharides (glucose, fructose, galactose) and disaccharides (saccharose, cellobiose, maltose, lactose) indicated that Hb retained by affinity onto CL-amylose columns, can be eluted only with galactose and lactose; with the other tested saccharides, very poor or no desorption at all, has been observed. These new data suggest: (1) a selective recognition of a limited number of (poly)saccharidic materials; and (2) a different behavior towards various sugars, the best interaction being observed with galactose-containing sugars (lactose). These aspects fit well with the hypothesis of a hemoglobin recognition center for sugars.

Amylose↗
PubMed2004

Solid-phase synthesis and 1H and 13C high-resolution magic angle spinning NMR of 13C-labeled resin-bound saccharides.

We show how high-resolution magic angle-spinning NMR spectroscopy can be used to characterize 13C-labeled saccharides that have been prepared using solid-phase synthesis techniques while they are still bound to a solid-support resin. With the use of 13C-labeled glucose as the starting material, we have successfully synthesized mono-, di- and trisaccharides with uniform 13C labeling of the saccharide rings. Using these materials, we have been able to assign the 13C and 1H spectra and to characterize various impurities on the resin beads.

Algorithms↗
PubMed1997

Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions.

The crystal structure of the maltodextrin-specific porin from Salmonella typhimurium ligated with a maltotrioside at the pore eyelet is known at 2.4 A resolution. The three glucose units assume a conformation close to the natural amylose helix. The pore eyelet fits exactly the cross-section of a maltooligosaccharide chain and thus functions as a constraining orifice. The oligomer permeates the membrane by screwing along the amylose helix through this orifice. Because each glucose glides along the given helix, its interactions can be sampled at any point along the pathway. The interactions are mostly hydrogen bonds, but also contacts to aromatic rings at one side of the pore. We have derived the energy profile of a gliding maltooligosaccharide by following formation and breakage of hydrogen bonds and by assessing the saccharide-aromatics interactions from a statistical analysis of saccharide binding sites in proteins. The resulting profile indicates smooth permeation despite extensive hydrogen bonding at the orifice.

Bacterial Outer Membrane Proteins↗
PubMed2005

A tandem mass spectrometric study of saccharides at high mass resolution.

Nine monosaccharides and four disaccharides were mass analyzed using a quadrupole time-of-flight tandem mass spectrometer combined with an electrospray ionization source. Product ion mass spectra of deprotonated, protonated, and sodiated saccharides were observed and were compared within each group of saccharides. Each of the deprotonated pentoses, hexoses and disaccharides yielded a significantly different product ion mass spectrum with the exception of alpha-lactose and beta-lactose. The disaccharides alpha- and beta-lactose differ only at the glycosidic linkage. Product ion mass spectra of protonated and sodiated alpha- and beta-lactose were indistinguishable also.

Disaccharides↗
PubMed2000

Naturally occurring anti-band 3 antibody binds to apoptotic human T-lymphoid cell line Jurkat through sialylated poly-N-acetyllactosaminyl saccharide chains on the cell surface.

Human T-lymphoid cell line Jurkat was treated with actinomycin D (ActD) and cycloheximide (CHX). The induction of apoptosis was confirmed by the chromatin condensation and DNA ladder fragmentation. Anti-band 3 IgG, purified from normal human plasma, bound to the ActD- or CHX-treated cells, and the binding was correlated to the degree of apoptosis. Antioxidants, N-acetylcysteine, pilloridine dithiocarbamate, and trolox, inhibited neither induction of DNA fragmentation of ActD-treated cells nor anti-band 3 IgG binding to ActD-treated cells, indicating that formation of the anti-band 3 IgG binding sites on the apoptotic cell surface is caused by nonoxidative mechanism. When Jurkat cells were treated with endo-beta-galactosidase to cleave sialylated poly-N-acetyllactosaminyl saccharide chains from the cell surface before induction of apoptosis, the binding of anti-band 3 IgG was abolished. The results indicate that sialylated poly-N-acetyllactosaminyl saccharide chains on the cell surface are requisite for the binding of anti-band 3 IgG to apoptotic cells.

Amino Sugars↗
PubMed2000

Deuterium nuclear spin-lattice relaxation times and quadrupolar coupling constants in isotopically labeled saccharides.

(13)C and (2)H spin-lattice relaxation times have been determined by inversion recovery in a range of site-specific (13)C- and (2)H-labeled saccharides under identical solution conditions, and the data were used to calculate deuterium nuclear quadrupolar coupling constants ((2)H NQCC) at specific sites within cyclic and acyclic forms in solution. (13)C T(1) values ranged from approximately 0.6 to 8.2 s, and (2)H T(1) values ranged from approximately 79 to 450 ms, depending on molecular structure (0.4 M sugar in 5 mM EDTA (disodium salt) in (2)H(2)O-depleted H(2)O, pH 4. 8, 30 degrees C). In addition to providing new information on (13)C and (2)H relaxation behavior of saccharides in solution, the resulting (2)H1 NQCC values reveal a dependency on anomeric configuration within aldopyranose rings, whereas (2)H NQCC values at other ring sites appear less sensitive to configuration at C1. In contrast, (2)H NQCC values at both anomeric and nonanomeric sites within aldofuranose rings appear to be influenced by anomeric configuration. These experimental observations were confirmed by density functional theory (DFT) calculations of (2)H NQCC values in model aldopyranosyl and aldofuranosyl rings.

Deuterium↗