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Analysis of herbicide residues in sugar beet and sugar.

A simple quantitative TLC method for the determination of the residues of herbicide inhibiting photosynthesis was compared with capillary GLC for the analysis of atrazine, chloridazone, lenacil, phenmedipham and desmedipham in sugar beet and sugar. No significant differences in the determination limit and precision of the two methods were found. Monitoring of herbicide residue levels in commercial sugar revealed low levels of atrazine (0.003 mg.kg-1 on average) in all the samples. This contamination level does not present a health hazard consumers.

Chromatography, Gas↗

Magnesium deficiency in sugar beets alters sugar partitioning and phloem loading in young mature leaves.

Magnesium deficiency has been reported to affect plant growth and biomass partitioning between root and shoot. The present work aims to identify how Mg deficiency alters carbon partitioning in sugar beet (Beta vulgaris L.) plants. Fresh biomass, Mg and sugar contents were followed in diverse organs over 20 days under Mg-sufficient and Mg-deficient conditions. At the end of the treatment, the aerial biomass, but not the root biomass, of Mg-deficient plants was lower compared to control plants. A clear inverse relationship between Mg and sugar contents in leaves was found. Mg deficiency promoted a marked increase in sucrose and starch accumulation in the uppermost expanded leaves, which also had the lowest content of Mg among all the leaves of the rosette. The oldest leaves maintained a higher Mg content. [14C]Sucrose labelling showed that sucrose export from the uppermost expanded leaves was inhibited. In contrast, sucrose export from the oldest leaves, which are close to, and export mainly to, the roots, was not restricted. In response to Mg deficiency, the BvSUT1 gene encoding a companion cell sucrose/H+ symporter was induced in the uppermost expanded leaves, but without further enhancement of sucrose loading into the phloem. The observed increase in BvSUT1 gene expression supports the idea that sucrose loading into the phloem is defective, resulting in its accumulation in the leaf.

Base Sequence↗

Isolation of ketoses or nonreducing sugars from a sugar mixture containing aldoses by aniline treatment.

A method for the isolation of ketoses and nonreducing sugars from sugar mixtures by the addition of aniline, in the presence of acetic acid as a catalyst, is described. The aldoses react readily to form aniline derivatives, which are then removed using standard procedures: extraction with organic solvents, and treatment with activated charcoal and with a cation-exchange resin. The ketoses and nonreducing sugars are retained in aqueous solution.

Acetates↗

A new class of sugar analogues for use in the investigation of sugar transport.

D-Mannose derivatives have been synthesised which are crosslinked through their C-4 hydroxyls to propyl-2-amine. Coupling to the amino group gave a fluorodinitrobenzene derivative, a nitroazidophenyl derivative and an azidosalicylamide derivative. Each of these derivatives was shown to have high affinity for the human erythrocyte sugar transport system. The affinity constant for the nitroazidophenyl derivative was not altered by temperature changes. In rat adipocytes treated with insulin, the affinity constants for the derivatives were up to 1000-fold lower than for the parent sugar. In the absence of insulin the affinity constants for the derivatives, but not for D-mannose, were 3-times higher than in insulin-treated cells. By preparation of radiolabelled derivatives we have shown that the compounds are not transported either by erythrocytes or by adipocytes. Thus the crosslinked sugars are good outside-specific analogues.

3-O-Methylglucose↗

Isolation of the homogeneous constituents from non-diffusible sugar-peptide (NSP) fraction originating from bovine plasma--I. Method of disruption of a sugar-peptide aggregate.

1. High molecular weight sugar-peptide aggregate contains 84--92% of sugar-peptide compounds of the whole non-diffusible sugar-peptide (NSP) fraction obtained from bovine blood plasma by the two-step dialysis method. 2. The aggregate can be resolved into various numbers, dependent on conditions, of electrophoretic homogeneous bands, which appeared to be heterogeneous in thin-layer chromatography on MN-Cellulose. 3. Electrophoresis in 5 M guanidine-hydrochloride allows the disruption of the aggregate and isolation of seven chromatographic and electrophoretic homogeneous constituents with different molecular weights and chemical characters.

Animals↗

A spoonful of sugar helps the medicine go down? Perspectives on the use of sugar in children's medicines.

This analysis examines the policy issues involved in the removal of sugar from paediatric medicines. It reports a study which investigates the perspectives of professionals, consumers, and the pharmaceutical industry. Interviews were conducted with: parents of children receiving long term medication, dental professionals involved in influencing policy or caring for such children, and drug companies who produce medication for long term use by children. Results showed that the parent group preferred the tablet over the liquid form of medication; this was also considered acceptable by the key dental professionals interviewed. The removal of sugar from liquid medicine (rather than the alternative use of smaller tablets) was not therefore a policy generally preferred by the groups involved in the issue. It was concluded that the singular concern of the dentist, doctors and pharmacists to remove sugar from liquid paediatric medicines was a reflection of their altruistic intentions. The limited biomedical perspective of clinically trained occupations prevented them from exploring the wider issues of the various needs of consumers. Thus, the analysis highlights the problems which have been introduced by professional dominance in the issue of medication caries.

Attitude of Health Personnel↗

Structures of the sugar chains of rabbit immunoglobulin G: occurrence of asparagine-linked sugar chains in Fab fragment.

The asparagine-linked sugar chains of rabbit immunoglobulin G (IgG) and its Fc and Fab fragments were quantitatively liberated from the polypeptide portions by hydrazinolysis followed by N-acetylation and NaB3H4 reduction. After fractionation by paper electrophoresis, lectin chromatography, and gel filtration, their structures were studied by sequential exoglycosidase digestion in combination with methylation analysis. Rabbit IgG was shown to contain 2.3 mol of asparagine-linked sugar chains per molecule distributed in both the Fc and Fab fragments. The sugar chains were of the biantennary complex type containing four cores: Man alpha 1----6(Man alpha 1----3)(+/- GlcNAc beta 1----4)Man beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)-GlcNAc. A total of 16 distinct neutral oligosaccharide structures was found after sialidase treatment. The galactose residue in the monogalactosylated oligosaccharides was present on either the alpha 1----3 or alpha 1----6 side of the trimannosyl core. The Fab fragments contained neutral, monosialylated, and disialylated oligosaccharides, whereas the Fc fragment contained only neutral and monosialylated structures. The oligosaccharides isolated from the Fab fragments also contained more galactose and bisecting N-acetylglucosamine residues than those from the Fc fragments.

Animals↗

Asparagine-linked sugar chains of fetuin: occurrence of tetrasialyl triantennary sugar chains containing the Gal beta 1----3GlcNAc sequence.

Asparagine-linked sugar chains were quantitatively released from fetuin by hydrazinolysis. Structural analysis of the sugar chains by sequential exoglycosidase digestion in combination with methylation analysis and Smith degradation revealed that most of them have typical biantennary (8%) and triantennary (74%) structures containing different amounts of N-acetylneuraminic acid residues. In addition, an unusual tetrasialyl triantennary sugar chain (17%) containing the Gal beta 1----3GlcNAc sequence in the outer chain moiety was detected, and its structure was elucidated as NeuAc alpha 2----3Gal beta 1----3(NeuAc alpha 2----6)-GlcNAc beta 1----4(NeuAc alpha 2----6Gal beta 1----4GlcNAc beta 1----2)Man alpha 1----3(NeuAc alpha 2----3Gal beta 1----4GlcNAc beta 1----2Man alpha 1----6)Man beta 1----4GlcNAc beta 1----4GlcNAc.

Acetylglucosamine↗

Reaction of folic acid with reducing sugars and sugar degradation products.

The reaction of folic acid with reducing sugars (nonenzymatic glycation) under conditions that can occur during food processing and preparation was studied by high-performance liquid chromatography with diode array detection. N-(p-Aminobenzoyl)-L-glutamic acid, a well-established oxidation product, was detected in the reaction mixtures. Furthermore, a new product was isolated and identified as N2-[1-(carboxyethyl)]folic acid (CEF). CEF was the main product that was formed by the nonenzymatic glycation of folic acid. For preparation, N2-[1-(carboxyethyl)]folic acid was obtained in high yields when folic acid and dihydroxyacetone (DHA), a sugar degradation product, were heated at 100 degrees C in phosphate buffer. Mixtures of folic acid and different sugars or DHA were heated under variation of reaction time and temperature, and CEF was quantified. Up to 50% of the vitamin was converted to CEF, with highest yields formed from maltose (49%) and lactose (43%).

Carbohydrates↗

Synthesis of conformationally constrained C-glycosyl alpha- and beta-amino acids and sugar-carbamino sugar hybrids via Diels-Alder reaction.

[structure: see text] Sugar-derived dienes undergo Diels-Alder reactions with methyl alpha-nitro acrylate and ethyl beta-nitro acrylate to form the corresponding cycloadducts which have been converted into conformationally constrained C-glycosyl alpha- and beta-amino acids. Further, these beta-amino acids are converted into sugar-carbamino sugar hybrid molecules.

Amino Acids↗

Theoretical model of the three-dimensional structure of a sugar-binding protein from Pyrococcus horikoshii: structural analysis and sugar-binding simulations.

The three-dimensional structure of a sugar-binding protein from the thermophilic archaea Pyrococcus horikoshii has been predicted by a homology modelling procedure and investigated for its stability and its ability to bind different sugars. The model was created by using as templates the three-dimensional structures of a maltodextrin-binding protein from Pyrococcus furiosus, a trehalose-maltose-binding protein from Thermococcus litoralis and a maltodextrin-binding protein from Escherichia coli. According to the suggestions from the CASP (Critical Assessment of Structure Prediction) meetings, the homology modelling strategy was applied by assessing an accurate multiple sequence alignment, based on the high structural conservation in the family of ATP-binding cassette transporters to which all these proteins belong. The model has been deposited in the Protein Data Bank with the code 1R25. According to the origin of the protein, several characteristics in the organization of the secondary-structure elements and in the distribution of polar and non-polar amino acids are very similar to those of thermophilic proteins, compared with proteins from mesophilic organisms, and are analysed in detail. Finally, a simulation of the binding of several sugars in the binding site of this protein is presented, and interactions with amino acids are highlighted in detail.

Amino Acid Sequence↗

The effect of increasing nucleotide-sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes.

Treatment of rat hepatocytes with 0.5 mM concentrations of uridine and cytidine results in increased cellular concentrations of UTP, UDP-sugars and CTP, whereas that of CMP-N-acetylneuraminate remained unchanged [Pels Rijcken, Overdijk, Van den Eijnden and Ferwerda (1993) Biochem. J. 293, 207-213]. The incorporation of radioactivity from 3H-labelled sugars into the cell-associated and secreted glycoconjugate fraction was influenced by these altered cellular concentrations of the nucleotides. For [3H]glucosamine, pretreatment with uridine resulted in a reduction of the glycosylation in both fractions. Increases in the secreted fractions were observed for fucose with both uridine and cytidine and for N-acetylglucosamine with uridine only. With [3H]N-acetylglucosamine, similar specific radioactivities for UDP-N-acetylhexosamine and CMP-N-acetylneuraminate were found, regardless of the pretreatment conditions. With [3H]N-acetylmannosamine, the specific radioactivity of CMP-N-acetylneuraminate showed an almost 2-fold increase on pretreatment. The latter increase did not result in an increased incorporation of radioactivity into the glycoconjugates. It was estimated that, in untreated cells, the ratio of radioactivity incorporated from [3H]glucosamine into glycoconjugate-bound N-acetylhexosamine and N-acetylneuraminate amounted to 2:3. In pretreated cells this ratio changed to approx. 2:1. Overall, the data show that pretreatment resulted in an increased incorporation of N-acetylhexosamine into cell-associated and secreted glycoconjugates, accompanied by a reduction in sialylation. It was concluded that an increased availability of UDP-N-acetylhexosamine caused the increased incorporation of N-acetylhexosamine. The elevated cytosolic level of UDP-N-acetylhexosamine (and of compounds like CMP) is suggested to impair the transport of CMP-acetylneuraminate to the Golgi, resulting in reduced sialylation. This study demonstrates that protein glycosylation can be regulated at the level of the availability of the various nucleotide-sugars in the Golgi lumen.

Acetylglucosamine↗

Characterization of a sugar-binding protein from Azospirillum brasilense mediating chemotaxis to and uptake of sugars.

Our approach to the isolation of plant-inducible bacterial genes of Azospirillum brasilense, based on the analysis of protein patterns of bacteria grown in the presence and in the absence of plant root exudates, led to the identification of an acidic 40 kDa protein. Cloning and sequencing analysis of the corresponding coding DNA region revealed the presence of two open reading frames transcribed in the same orientation. The deduced ORF1 protein, which corresponds to the 40 kDa protein, is very similar to the periplasmic ChvE protein, identified in Agrobacterium tumefaciens and involved in enhanced virulence. The deduced ORF2 protein shows homology to members of the LysR family of transcriptional regulators. The function of the ChvE-like protein in A. brasilense was investigated further. The protein, designated as SbpA (sugar binding protein A), is involved in the uptake of D-galactose and functions in the chemotaxis of A. brasilense towards several sugars, including D-galactose, L-arabinose and D-fucose. Expression of the sbpA gene requires the presence of the same sugars in the growth medium and is enhanced further in combination with carbon starvation of A. brasilense cells.

Agrobacterium tumefaciens↗

The Asn-420-linked sugar chain in human epidermal growth factor receptor suppresses ligand-independent spontaneous oligomerization. Possible role of a specific sugar chain in controllable receptor activation.

To elucidate a role(s) of Asn-linked sugar chain(s) in the function of epidermal growth factor receptor (EGFR), a series of the EGFR mutants were prepared in which potential glycosylation sites in the domain III were eliminated by site-directed mutagenesis. Although the wild-type and mutants of Asn-328, Asn-337, and Asn-389 underwent autophosphorylation in response to epidermal growth factor (EGF), the Asn-420 --> Gln mutant was found to be constitutively tyrosine-phosphorylated. This abnormal ligand-independent phosphorylation of the mutant appears to be due to a ligand-independent spontaneous oligomer formation, as shown by a cross-linking experiment using the purified soluble extracellular domain (sEGFR). As revealed by the dissociation of the Asn-420 --> Gln sEGFR oligomer by simple dilution, it seems likely that the equilibrium is shifted toward oligomer formation to an unusual degree. Furthermore, it was also found that the mutation caused a loss of the ability to bind EGF. These findings suggest that the sugar chain linked to Asn-420 plays a crucial role in EGF binding and prevents spontaneous oligomerization of the EGFR, which may otherwise lead to uncontrollable receptor activation, and support the view of a specific role of an Asn-linked sugar chain in the function of a glycoprotein.

Asparagine↗

DNA duplexes containing altered sugar residues as probes of EcoRII and MvaI endonuclease interactions with sugar-phosphate backbone.

Oligonucleotides containing 1-(beta-D-2'-deoxy-threo-pentofuranosyl)cytosine (dCx) and/or 1-(beta-D-2'-deoxy-threo-pentofuranosyl)thymine (dTx) in place of dC and dT residues in the EcoRII and MvaI recognition site CC(A/T)GG were synthesized in order to investigate specific recognition of the DNA sugar-phosphate backbone by EcoRII and MvaI restriction endonucleases. In 2'-deoxyxylosyl moieties of dCx and dTx, 3'-hydroxyl groups were inverted, which perturbs the related individual phosphates. Introduction of a single 2'-deoxyxylosyl moiety into a dC x dG pair resulted in a minor destabilization of double-stranded DNA structure. In the case of a dA x dT pair the effect of a 2'-deoxyxylose incorporation was much more pronounced. Multiple dCx modifications and their combination with dTx did not enhance the destabilization effect. Hydrolysis of dCx-containing DNA duplexes by EcoRII endonuclease was blocked and binding affinity was strongly depended on the location of an altered sugar. A DNA duplex containing a dTx residue was cleaved by the enzyme, but kcat/K(M) was slightly reduced. In contrast, MvaI endonuclease efficiently cleaved both types of sugar-altered substrate analogs. However it did not cleave conformationally perturbed scissile bonds, when the corresponding unmodified bonds were perfectly hydrolyzed in the same DNA duplexes. Based on these data the possible contributions of individual phosphates in the recognition site to substrate recognition and catalysis by EcoRII were proposed. We observed strikingly non-equivalent inputs for different phosphates with respect to their effect on EcoRII-DNA complex formation.

Carbohydrates↗

[The energetic utilization of sugar beets, dried chips, cane sugar and apple pectin by growing swine. 2. Nitrogen and energy metabolism].

The energetic utilization of rations with raw and steamed sugar beets, dried sugar beet pulp (16 measured values each), sucrose and apple pectin (8 measured values each) as supplement feed to a basic ration was measured at 4 growing pigs each in the live weight range of between 40 and 130 kg. The utilization of the energy in the rations amounted to 69.1 +/- 5.5, 68.3 +/- 7.1, 60.9 +/- 5.8, 70.5 +/- 4.1 and 69.9 +/- 6.9% (same sequence as above). The utilization values for the supplemented feedstuffs were 69.2 +/- 7.4, 68.0 +/- 10.0, 55.9 +/- 9.7, 72.2 +/- 7.6 and 71.7 +/- 17.3%. The average retention value of the digestible pectin was derived from the test results with dried sugar beet pulp and apple pectin as 5.8 kJ/g. An influence of the ontogenetic development on energy utilization cannot be derived from the comparison of the retention effect of digestible nutrients measured at growing pigs and that derived from adult pigs.

Animal Feed↗

Active sugar transport by the small intestine. The effects of sugars, amino acids, hexosamines, sulfhydryl-reacting compounds, and cations on the preferential binding of D-glucose to tris-disrupted brush borders.

Tris-disrupted and intact brush border membrane preparations from mucosa of hamster jejunum were capable of preferentially binding actively transported D-glucose in a similar manner. Density gradient centrifugation of the Tris-disrupted brush borders indicated that D-glucose was bound to a fraction containing the cores or inner material of the microvilli. The properties of this binding were examined with the Tris-disrupted brush border preparation. Actively transported sugars competitively inhibited preferential D-glucose binding, whereas no effect was observed with nonactively transported sugars. Neither actively nor nonactively transported amino acids affected D-glucose binding. D-Glucosamine, which is not actively transported, was inhibitory to preferential D-glucose binding as well as to the active transport of D-glucose by everted sacs of hamster jejunum. No inhibitory effect was observed with the same concentration of D-galactosamine. Preferential D-glucose binding was also inhibited by sulfhydryl-reacting compounds, Ca(2+), and Li(+) ions. On the other hand, Mg(2+) was shown to be stimulatory and Na(+), NH(4) (+), and K(+) had no effect on this phenomenon. The results of these experiments suggest that preferential D-glucose binding to brush borders is related to the initial step in active sugar transport by the small intestine.

Amino Acids↗

Evaluation of health aspects of sugars contained in carbohydrate sweeteners. Report of Sugars Task Force, 1986.

A critical review composed of two parts: estimates of present levels of sugars intake and of recent trends in nutritive carbohydrate sweetener content of the food supply and a review of recent scientific literature addressing potentially adverse health effects associated with sugars consumption. The review contains an executive summary, an appendix with 75 tables summarizing the estimation of sugars intake of U.S. population groups, and over one thousand citations.

Animals↗