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PubMed1989

Anti-thrombin activities of heparin. Effect of saccharide chain length on thrombin inhibition by heparin cofactor II and by antithrombin.

The interactions of two proteinase inhibitors, heparin cofactor II and antithrombin, with thrombin are potentiated by heparin. Using two methods, we have studied the potentiating effects of a series of heparin (poly)saccharides with high affinity for antithrombin and mean Mr ranging from approx. 1700 to 18,800. First, catalytic amounts of heparin (poly)saccharide were added to purified systems containing thrombin and either heparin cofactor II or antithrombin. Residual thrombin activity was determined with a chromogenic substrate. It was found that only the higher-Mr polysaccharides (Mr greater than 8000) efficiently catalysed thrombin inhibition by heparin cofactor II, there being a progressive catalytic effect with increasing Mr of the polysaccharide. Weak accelerating effects were noted with low-Mr saccharides (Mr less than 8000). This contrasted with the well-characterized interaction of heparin with antithrombin and thrombin, where heparin oligosaccharides of Mr less than 5400 had absolutely no ability to accelerate the reaction, while (poly)saccharides of Mr exceeding 5400 showed rapidly increasing catalytic activity with increasing Mr. Secondly, these and other heparin preparations were added in a wide concentration range to plasma with which 125I-labelled thrombin was then incubated for 30 s. Inhibited thrombin was determined from the distribution of labelled thrombin amongst inhibitor-thrombin complexes, predominantly antithrombin-thrombin and heparin cofactor II-thrombin complexes. In this situation, where the inhibitors competed for thrombin and for the (poly)saccharides, it was found that, provided the latter were of high affinity for antithrombin and exceeded a Mr of 5400, thrombin inhibition in plasma was mediated largely through antithrombin. Polysaccharides of Mr exceeding 8000 that were of low affinity for antithrombin accelerated thrombin inhibition in plasma through their interaction with heparin cofactor II. High concentrations of saccharides of Mr 1700-5400 exhibited a size-dependent acceleration of thrombin inhibition, not through their interaction with antithrombin, but through their interaction with heparin cofactor II.

Antithrombins↗

PubMed2004

Protection of protein secondary structure by saccharides of different molecular weights during freeze-drying.

The protective effects of saccharides with various molecular weights (glucose, maltose, maltotriose, maltotetraose, maltopentaose, maltoheptaose, dextran 1060, dextran 4900, and dextran 10200) against lyophilization-induced structural perturbation of model proteins (BSA, ovalbumin) were studied. Fourier transform infrared (FT-IR) analysis of the proteins in initial solutions and freeze-dried solids indicated that maltose conferred the greatest protection against secondary structure change. The structure-stabilizing effect of maltooligosaccharides decreased in increasing the number of saccharide units. Larger molecules of dextran also showed a smaller structure-stabilizing effect. Increasing the effective saccharide molecular size by a borate-saccharide complexation reduced the protein structure-stabilizing effect of all of the saccharides except glucose. The results indicate that the larger saccharide molecules, and/or the complex formation with borate ion, reduce the free and accessible hydroxyl groups to interact with and stabilize the protein structure by a water-substitution mechanism.

Calorimetry, Differential Scanning↗

PubMed2000

[Effect of processing contents of saccharides in Danggui].

OBJECTIVE: To explore the effect of processing on the contents of saccharides in Danggui. METHOD: The contents of reducing saccharides, water-soluble saccharides and poly saccharides in Danggui and its processed products were determined by phenol-H2SO4 method. RESULTS: The contents of saccharides in the alcohol-broiled product were higher than those in the crude drug. CONCLUSION: Different processing methods have significant effects on the above saccharides, which administers to the interpreparation of the theory of Danggui processing.

Angelica sinensis↗

PubMed2003

[Effects of processing on contents of saccharides in huangqi].

OBJECTIVE: To explore the effect of processing on the contents of saccharides in Huangqi. METHOD: The contents of reducing saccharides, water-soluble saccharides and poly saccharides in Huangqi and its processed products were determined with phenol-H2SO4 method. RESULT: The contents of poly saccharides in the alcohol-broiled product were the highest of all the products. The others were all higher than those in the crude drug. CONCLUSION: Different processing methods result in different effects on the above saccharides, which administers to the interpretation of the theory of Huangqi processing.

Astragalus propinquus↗

PubMed2000

Determination of saccharides in sake by high-performance liquid chromatography with polarized photometric detection.

A high-performance liquid chromatographic method has been developed for the determination of saccharides in sake, an alcoholic beverage brewed from rice. Saccharides in sake were separated on a normal phase (carbamoyl bonded silica) column using a linear gradient elution of water in acetonitrile. Seven saccharides, glucose, maltose, isomaltose, maltotriose, panose, isomaltotriose and ethyl alpha-D-glucoside, were determined by a polarized photometric detector. Unidentified peaks suggesting saccharides with polymerization degrees over 4 were also observed. The proposed method did not require any sample clean-up treatment. As an application, saccharide compositions in various kinds of sake were compared.

Beverages↗

PubMed2000

The three-dimensional structure of the 4:1 mithramycin:d(ACCCGGGT)(2) complex: evidence for an interaction between the E saccharides.

Mithramycin and chromomycin, two antitumor drugs, each having an identical aglycone and nearly identical disaccharide and trisaccharide side chains, have differing binding properties to a small oligonucleotide, d(ACCCGGGT)(2) (M. A. Keniry et al., Journal of Molecular Biology, 1993, Vol. 231, pp. 753-767). In order to understand the forces that induce four mithramycin molecules to bind to d(ACCCGGGT)(2) instead of two drug molecules in the case of chromomycin, the structure of the 4:2:1 mithramycin: Mg(2+):d(ACCCGGGT)(2) complex was investigated by (1)H-nmr and restrained molecular dynamics. The resulting three-dimensional model showed that in order to accommodate the close approach of one neighboring mithramycin dimer, the inwardly directed CDE saccharide chain of the neighboring mithramycin dimer undergoes a conformational change such that the E saccharide no longer spans the minor groove but reorients so that the hydrophilic face of the E saccharides from the two dimers oppose each other. Two hydrogen bonds are formed between the hydroxyl groups of the two opposing E saccharide groups. The results are interpreted in terms of the differences in stereochemistry and functional group substitutions between mithramycin and chromomycin. A mithramycin dimer is able to self-associate on an oligonucleotide template because it has two hydroxyl groups on the same face of its terminal E saccharide. A chromomycin dimer is unable to self-associate because one of these hydroxyl groups is acetylated and the neighboring hydroxyl group has a stereochemistry that cannot permit close contact of the hydroxyl group with a neighbouring chromomycin dimer.

Antibiotics, Antineoplastic↗

PubMed2003

Construction of artificial signal transducers on a lectin surface by post-photoaffinity-labeling modification for fluorescent saccharide biosensors.

A new general method, post-photoaffinity-labeling modification (PPALM), for constructing fluorescent saccharide biosensors based on naturally occurring saccharide-binding proteins, lectins, is described in detail. An active-site-directed incorporation of a masked reactive site into a lectin was conducted by using a photoaffinity labeling technique followed by demasking and then chemical modification to yield a fluorescent lectin. Two photoaffinity labeling reagents were designed and synthesized in this study. The labeling reagent with a photoreactive site appended through a disulfide link to a mannoside unit was bound to the saccharide-binding pocket of the lectin concanavalin A (Con A). After light irradiation, the mannoside unit was cleaved by reduction. The unique thiol group thus produced was site-specifically modified with various fluorescent groups (dansyl, coumarin, or dimethylaminobenzoate derivatives) to afford fluorescent Con As. The labeling site was characterized by protease-catalyzed digestion followed by HPLC, MALDI-TOF MS, and tandem mass-mass spectrometry; these methods indicated that the photolabeling step is remarkably site specific. Strong fluorescence was observed in the engineered Con A with a fluorophore, and the emission changed sensitively upon saccharide complexation. The binding constants for various saccharides were determined by fluorescence titration and demonstrated that the binding selectivity and affinity of the engineered Con As are comparable to those of native Con A. The red shift of the emission maximum, the decrease in the fluorescence anisotropy of the dansyl unit, and the increase in the twisted intramolecular charge transfer emission caused by sugar binding to the engineered Con A explicitly indicate that the microenvironment of the appended fluorophores changes from a restricted and relatively hydrophobic environment into a rather freely mobile and hydrophilic environment.

Binding Sites↗

PubMed1996

Effect of Saccharides on the Glass-Forming Tendency and Stability of Solutions of 2,3-Butanediol, 1,2-Propanediol, or 1,3-Butanediol in Water, Phosphate-Buffered Saline, Euro-Collins Solution, or Saint Thomas Cardioplegic Solution

The effect of sugars or reduced saccharides trehalose, sucrose, sorbitol, or mannitol on the glass-forming tendency during cooling and the stability of the wholly amorphous state during warming has been studied with 2,3-butanediol, 1,2-propanediol, or 1,3-butanediol in three different carrier solutions. The 2,3-butanediol contained 96.7% (w/w) racemic mixture of the levo and dextro isomers and 3.1% (w/w) of the meso isomer (called 2,3-butanediol 97% dl). The carrier solutions were water, a phosphate-buffered saline, and two organ preservation solutions (Euro-Collins and Saint Thomas). The latter two were chosen because they are often used for kidney and heart preservation, respectively. The concentrations of 2,3-butanediol, 1,2-propanediol, and 1,3-butanediol varied respectively from 25 to 34, 30 to 35, and 30% (w/w). The concentrations of saccharides were 4 or 5% (w/w). In the absence of saccharides, for a given 2,3-butanediol concentration, the glass-forming tendency increased in the following order: water, Saint Thomas, the phosphate buffer, Euro-Collins. Addition of 4 or 5% (w/w) saccharide resulted in a large increase in the glass-forming ability of the solution during cooling and increased the stability of the glass during warming; but replacement of 4 or 5% diol by an equivalent weight (percentage) of a saccharide decreased, though to a lesser extent, these properties.

Journal Article↗

PubMed1984

Mineralization of 2,4-dichlorophenoxyacetic acid in soil simultaneously enriched with saccharides.

Detoxication of 2,4-dichlorophenoxyacetic acid (2,4-D) in samples of chernozem soil was determined by a biological test and the time course of production of 14CO2, a product of microbial degradation of 2-14C-2-4-D, was measured during 38-d incubation at 28 degrees C in the dark. Enrichment of the soil with glucose (1000 ppm), two exocellular bacterial glucan and glucomannan polysaccharides (750 ppm), or a mixture of glucose with (NH4)2SO4 (C : N = 5 : 1) brought about acceleration of both detoxication and mineralization of 2,4-D (50 ppm) added simultaneously with the saccharides. Mineralization of the saccharides always preceded the degradation of the herbicide. The lag phase of 2,4-D mineralization did not exceed 3 d. In samples with saccharides the doubling time of the mineralization activity in the exponential phase of the process was substantially shortened and the mineralization of 2,4-D was accelerated even when the soil was inoculated with a suspension of soil in which microbial 2,4-D decomposers had accumulated. The extent of mineralization was not affected by the presence of saccharides (about 1/3 of the introduced radioactive carbon was transformed into 14CO2). All saccharides had a similar effect which reflected an increase in the overall bacterial count and in the relative abundance of bacterial 2,4-D decomposers . The role of other mechanisms such as co-metabolism in the stimulation of the degradation process is discussed.

2,4-Dichlorophenoxyacetic Acid↗

PubMed2005

Distinction between some saccharides in scattered optical sum frequency intensity images.

Using an optical sum frequency (SF) microscope with visible and infrared light pulses for excitation, we have attempted to distinguish among four saccharide species. The saccharides we studied were d-glucose, amylopectin, beta-cyclodextrin, and amylose. The wavelength of the infrared light was resonant to CH vibration. Amylose showed very weak sum frequency scattering for CH vibration among the four saccharides. As for the other three saccharides, we found a big difference in the sum frequency spectra of their CH stretching vibration near 2900 cm-1, when the incident visible and infrared light pulses were p- and s-polarized, respectively. Based on these facts, we have demonstrated a distinction between these three saccharides in the scattered SF intensity images.

Amylopectin↗

PubMed1991

Determination of saccharides in biological materials by high-performance anion-exchange chromatography with pulsed amperometric detection.

High-performance anion-exchange chromatography (HPAEC) coupled with pulsed amperometric detection (PAD) under alkaline conditions (pH 9-13) separates aminosaccharides, neutral saccharides and glycuronic acids based upon their molecular size, saccharide composition and glycosidic linkages. Carbohydrates were extracted by utilizing 0.5 M H2SO4 (neutral monosaccharides), 0.25 M H2SO4 coupled with enzyme catalysis (glycuronic acids) and 3 M H2SO4 (aminosaccharides). Solid-phase extraction with strong cation and strong anion resins was used to partition the cationic aminosaccharides and anionic glycuronic acids and to deionize acid extracts for neutral saccharides. Separation was conducted on a medium-capacity anion-exchange column (36 mequiv.) utilizing sodium hydroxide (5-200 mM and sodium acetate (0-250 mM) as the mobile phase. The saccharides were detected by oxidation at a gold working electrode with triple-pulsed amperometry. HPAEC-PAD was found superior to high-performance liquid chromatography with refractive index (RI) detection for neutral monosaccharides and aminosaccharides and to low-wavelength UV detection for glycuronic acids in terms of resolution and sensitivity. HPAEC-PAD was not subject to interferences as was the case for low UV detection (210 nm) or RI analyses and was highly selective for mono- and aminosaccharides and glycuronic acids. The use of HPAEC-PAD was applied for the determination of the saccharide composition of organic materials (plant residues, animal wastes and sewage sludge), microbial polymers and soil.

Animals↗

PubMed2002

Gustatory responsiveness to food-associated saccharides in European rabbits, Oryctolagus cuniculus.

Taste preference thresholds for six food-associated saccharides and relative sweet-taste preferences were assessed in 12 European rabbits using two-bottle choice tests of brief duration (3 min). In Experiment 1, the animals were found to significantly prefer concentrations as low as 30 mM maltose, 50 mM polycose and sucrose, 75 mM glucose, 150 mM fructose, and 175 mM lactose over tap water. In Experiment 2, the rabbits were given a choice between all binary combinations of the same six saccharides presented in equimolar concentrations of 100 and 200 mM. Preferences for individual saccharides were stable across the concentrations tested and indicate the following order of relative effectiveness: maltose=polycose>sucrose>glucose>fructose > or =lactose. The results showed rabbits to display a pattern of taste preference thresholds and relative taste preferences for food-associated saccharides similar to that found in rodents but differing markedly from that found in human and nonhuman primates. The results support the assumptions that rabbits, unlike most primates, but similar to rodents, may have specialized taste receptors for starch, and that the gustatory responsiveness of Oryctolagus cuniculus to food-associated saccharides might reflect an evolutionary adaptation to its dietary habits.

Animals↗

PubMed1999

Fibroblast growth factor receptor signalling is dictated by specific heparan sulphate saccharides.

Signalling by fibroblast growth factors (FGFs) through FGF receptors (FGFRs) depends on the cell-surface polysaccharide heparan sulphate (HS) [1] [2]. HS has an ordered domain structure of highly diverse saccharide motifs that present unique displays of sulphate, carboxyl and hydroxyl groups [3]. These motifs interact with many proteins, particularly growth factors. HS binds both to FGFs [4] [5] [6] and FGFRs [7], and probably activates signalling by facilitating ligand-induced receptor dimerisation [8] [9]. Nevertheless, the extent to which specific HS saccharide sequences play a regulatory role has not been established. By screening a library of structurally diverse HS decasaccharides in bioassays of FGF signalling mediated by three different FGFR isoforms, we found that saccharides showed specificity for both ligands and receptors; some saccharides selectively activated FGF signalling through different FGFR isoforms, others acted as negative regulators. We conclude that HS saccharides play critical roles in dictating the specificity of ligand-receptor interactions in FGFR signalling. Controlled alterations in HS structures [10] would provide a mechanism for regulation of cellular responsiveness to growth factors that bind HS.

Animals↗

PubMed1998

FT infrared and Raman investigation of saccharide-phosphatidylcholine interactions using novel structure probes.

Conformational consequences of adduct formation between saccharides (trehalose, glucose, raffinose) and sorbitol with dipalmitoylphosphatidylcholine (DPPC) in multibilayers are revealed by relative intensity changes of the band components corresponding to the nu asN(CH3)3 and nu sC-N(CH3)3 stretching modes of the choline chain terminal and those of the nu C = O band. The conformational sensitivity of those modes was demonstrated previously (J. Grdadolnik et al., Chem. Phys. Lipids 65 (1993) 121) and used to demonstrate the effects of stepwise hydration of phosphatidylcholines. The latter are compared with the effects of saccharide binding and found to be qualitatively similar, but not identical. The same is true of the low frequency shifts of the nu asPO2- vibration: the shifts due to saccharide binding correspond to the binding of six to seven water molecules per phosphate which is about 20 cm-1 less than the shift caused by full hydration. A particularly interesting finding concerns the appearance of two bands in the nu asPO2- region of the DPPC-saccharide adducts. The relative intensities of the two bands (1243 and 1223 cm-1) change on additional hydration; it is the one at 1223 cm-1 that prevails at high hydration levels. Major changes in saccharide conformation are not detectable but minor differences between the DPPC bound and crystal spectra are observed.

1,2-Dipalmitoylphosphatidylcholine↗

PubMed2002

Lectin-erythrocyte interaction with external transmembrane glycophorin saccharides controlling membrane internal cytoskeleta.

Human red blood cell (RBC, erythrocyte) membranes have internal protein skeletons that govern the cells' distinctive discocyte-echinocyte morphology (shape) changes, seen in conventional microscopy. Glycophorin, the cell's transmembrane protein, presents all of its saccharides outside the cell. The protein sector of glycophorin is linked inside to the RBC cytoskeleton, enabling lectins binding to the external saccharides to gain profound control over internal cytoskeleton behavior, expressed by governance of the visibly seen cell shape. Critical lectin binding stoichiometries ((125)I-labeled lectins) equate to the number of glycophorin monomers per RBC, 7 x 10(5) copies/cell. Wheat germ agglutinin lectin (sialic acid specific) binds to glycophorin's outermost (exo) saccharides and exerts tight control over the cell's morphology. Removal of sialic acid groups (desialation) exposes the endosaccharides of glycophorin, enabling peanut agglutinin and Osage orange lectins to gain equally tight control over the RBC's morphology behavior in simple stoichiometric ratios, bound lectin molecules/glycophorin receptor. Thus, lectin specificities for saccharides are sharply in register with the glycophorin external saccharide composition, the sequence along the chains, and the number of copies of protein (stoichiometry). These relationships were determined via RBC shape change equilibria and also via shape change rates. Rate data are somewhat laborious to determine, but are exquisitely sensitive to lectin specificities and in very small lectin concentrations. Both classes of data enable these interactions to be analyzed in lectin and RBC concentrations approximately 100-fold smaller than agglutinating levels.

Carbohydrate Metabolism↗

PubMed1999

Role of saccharides on lung preservation.

BACKGROUND: Saccharides are considered to play a role as osmotic impermeants and serve as an energy source for the organ during ischemia. However, previous studies on the effectiveness of saccharides on organ preservation have yielded conflicting results. We compared the preservative effects of a monosaccharide (glucose), disaccharides (trehalose, maltose, sucrose), and a trisaccharide (raffinose) to investigate whether the effects of saccharides on lung preservation depend on their molecular weight, energy-level maintenance, and cytoprotective effects. METHODS: We used an ex vivo rat lung model using homologous blood as the perfusate. In the fresh group, the lungs were reperfused immediately after flush. In the other groups, the lungs were flushed with one of the solutions containing glucose, trehalose, maltose, sucrose, or raffinose and preserved for 14 hours. RESULTS: The results of the trehalose group were comparable to those of the fresh group. The glucose, maltose, and raffinose groups showed significantly higher levels of shunt fraction, pulmonary artery pressure, and peak inspiratory pressure compared with the fresh and trehalose groups. There were no differences among the groups in the levels of total adenine nucleotides, adenosine triphosphate of the lung after flush, and preservation. However, after reperfusion, levels of total adenine nucleotides became significantly lower in the glucose, sucrose, maltose, and raffinose groups. Ultrastructural examination revealed endothelial cell injury in the glucose, sucrose, maltose, and raffinose groups. CONCLUSIONS: These results show that the effects of saccharides may depend on their cytoprotective effect rather than on impermeant activity or energy-level maintenance of the preserved lung. Trehalose proved to be superior to the other saccharides.

Adenine Nucleotides↗

PubMed1978

Lectin analysis of Trypanosoma congolense bloodstream trypomastigote and culture procyclic surface saccharides by agglutination and electron microscopic technics.

Living, intact bloodstream trypomastigotes and culture procyclic forms of Trypanosoma congolense were tested for aggulination with the lectins concanavalin A (Con A), phytohemagglutinin P (PP), wheat germ agglutinin (WGA), soybean agglutinin (SBA), and fucose binding protein (FBP). Similar experiments were conducted with living bloodstream and culture forms treated with trypsin or dextranase. Parasites were incubated for 30 min at 25 C in various concentrations of each lectin, then examined for agglutination by dark-field microscopy. Control preparations consisted of parasites incubated alone or with 0.5 M of the specific competing sugar, with or without the corresponding lectin. Electron-microscopic localization of lectin binding sites on the surface of intact and dextranase-treated bloodstream and intact culture forms was accomplished with Con A, reacted with horseradish peroxidase (HRP) and then diaminobenzidine (DAB). In addition, FBP and SBA were coupled to HRP, then utilized for the localization of binding saccharides on the surface of bloodstream forms by the DAB technic. Similar studies were conducted with culture procyclics incubated with WGA-, SBA-, PP- or FBP-HRP conjugates and then reacted with DAB. Controls were utilized to confirm the sugar specificity of all positive reactions. Intact living bloodstream forms were agglutinated in a concentration-dependent manner with all the lectins tested. Agglutination levels were scored as Con A greater than FBP greater than WGA = PP = SBA. Sugars resembling alpha-D-mannose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, and alpha-L-fucose are evidently present on the surface of the parasites. No agglutination was noted in any control preparations. Identical lectin-induced agglutinations were obtained with trypsin- or dextranase-treated bloodstream forms. Trypsin disrupted but did not entirely remove the surface coat of bloodstream forms, while dextranase did not alter the ultrastructure of the parasites. Con A-, SBA- and FBP-binding saccharides were distributed uniformly on the surface coat of intact bloodstream forms; a similar distribution of Con A receptors was noted also on the surface of dextranase-treated cells. No lectin-binding saccharides were visualized by electron microscopy on any control preparations. Intact, trypsin- or dextranase-treated, procyclics were agglutinated in a concentration-dependent fashion by Con A and WGA, but not by the other lectins tested. Control preparations did not agglutinate and the enzymes did not affect the ultrastructure of the parasites. Con A- and WGA-specifically binding saccharides were uniformly distributed on intact procyclics and control preparations were lectin-negative. Thus, T. congolense procyclics retained surface saccharides resembling alpha-D-mannose and N-acetyl-D-glucosamine but lost sugars resembling N-acetyl-D-galactosamine (or D-galactose) and alpha-L-fucose...

Agglutination Tests↗

PubMed1994

Tissue-targeting ability of saccharide-poly(L-lysine) conjugates.

To evaluate the effect of introducing a saccharide moiety to poly(amino acids) on tissue distribution, several glycoconjugates of epsilon-(2-methoxyethoxyacetyl)-poly(L-lysine) of three molecular weights were synthesized using an octylene spacer between the sugar and polymer chain. Methoxyethoxyacetylation of the epsilon-amino group of the lysine unit in poly(L-lysine) was useful for avoiding nonspecific distribution to many tissues as the result of cationic charges. The tissue-targeting ability of each saccharide moiety was considered as the actual amount changed in each tissue caused by saccharide modification. Galactose terminated saccharides such as galactose, lactose and N-acetylgalactosamine accumulated exclusively in the liver, probably by the hepatic receptor. These conjugates could therefore be good carriers for a drug delivery system to the liver. On the other hand, the mannosyl and fucosyl conjugates were preferentially delivered to the reticuloendothelial systems such as those in the liver, spleen and bone marrow. In particular, fucosyl conjugates accumulated more in the bone marrow than in the spleen. Xylosyl conjugates accumulated mostly in the liver and lung. Generally, the accumulated amount in the target tissue increased with increasing molecular weight and an increased number of saccharides on one molecule of polymer.

Animals↗