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At least 73 records · Page 4Linked to original sources
PubMed1982

Sugar availability, sugar consumption and dental caries.

This study was conducted to update our knowledge about the relation between sugar consumption and dental caries in nations throughout the world. Data on the prevalence of dental caries for 6- and 12-year-old children in, respectively, 23 and 47 nations were obtained from the World Health Organization's Global Oral Epidemiology Bank. Information on sugar supplies was obtained from Food Balance Sheet data prepared by the Food and Agriculture Organization of the United Nations. The study indicates that for the 12-, but not for the 6-, year-old-children there is a significant positive correlation between the per capita availability of sugar and dental caries. The data also suggest that the availability, and presumably the ingestion, of 50 g of sugar per day may represent an outer limit of "safe" or "acceptable" sugar consumption. Furthermore, a comparison of data obtained from Food Balance Sheets for the per capita daily "consumption" of sugar with data for consumption obtained from Household Consumption Surveys in six countries, shows that these data collection methods frequently do not give comparable results. Accurate, total, age-specific consumption figures with information on frequency and the manner of use are needed if the relationship between oral disease and dietary sugar is to be clarified.

Child↗
PubMed2002

Respiration-dependent utilization of sugars in yeasts: a determinant role for sugar transporters.

In many yeast species, including Kluyveromyces lactis, growth on certain sugars (such as galactose, raffinose, and maltose) occurs only under respiratory conditions. If respiration is blocked by inhibitors, mutation, or anaerobiosis, growth does not take place. This apparent dependence on respiration for the utilization of certain sugars has often been suspected to be associated with the mechanism of the sugar uptake step. We hypothesized that in many yeast species, the permease activities for these sugars are not sufficient to ensure the high substrate flow that is necessary for fermentative growth. By introducing additional sugar permease genes, we have obtained K. lactis strains that were capable of growing on galactose and raffinose in the absence of respiration. High dosages of both the permease and maltase genes were indeed necessary for K. lactis cells to grow on maltose in the absence of respiration. These results strongly suggest that the sugar uptake step is the major bottleneck in the fermentative assimilation of certain sugars in K. lactis and probably in many other yeasts.

Anaerobiosis↗
PubMed2004

A sugar beet chlorophyll a/b binding protein promoter void of G-box like elements confers strong and leaf specific reporter gene expression in transgenic sugar beet.

BACKGROUND: Modification of leaf traits in sugar beet requires a strong leaf specific promoter. With such a promoter, expression in taproots can be avoided which may otherwise take away available energy resources for sugar accumulation. RESULTS: Suppression Subtractive Hybridization (SSH) was utilized to generate an enriched and equalized cDNA library for leaf expressed genes from sugar beet. Fourteen cDNA fragments corresponding to thirteen different genes were isolated. Northern blot analysis indicates the desired tissue specificity of these genes. The promoters for two chlorophyll a/b binding protein genes (Bvcab11 and Bvcab12) were isolated, linked to reporter genes, and transformed into sugar beet using promoter reporter gene fusions. Transient and transgenic analysis indicate that both promoters direct leaf specific gene expression. A bioinformatic analysis revealed that the Bvcab11 promoter is void of G-box like regulatory elements with a palindromic ACGT core sequence. The data indicate that the presence of a G-box element is not a prerequisite for leaf specific and light induced gene expression in sugar beet. CONCLUSIONS: This work shows that SSH can be successfully employed for the identification and subsequent isolation of tissue specific sugar beet promoters. These promoters are shown to drive strong leaf specific gene expression in transgenic sugar beet. The application of these promoters for expressing resistance improving genes against foliar diseases is discussed.

Beta vulgaris↗
PubMed1987

Equilibrium ligand binding to the human erythrocyte sugar transporter. Evidence for two sugar-binding sites per carrier.

Equilibrium [3H]cytochalasin B binding to class I sites of human red cell membranes (the sugar transporter) was examined in the presence and absence of intracellular or extracellular sugars known to interact with the transport system. D-Glucose, a transported sugar, is without effect on cytochalasin B binding when present in the extracellular medium but is an effective inhibitor of binding when present within the cell. Ethylidene glucose and maltose (reactive but nontransported sugars) inhibit cytochalasin B (CCB) binding when present either outside or inside the red cell. Inhibition by intracellular sugar (Si) is of the simple, linear competitive type. Inhibition by extracellular sugars (So) is more complex; the Kd(app) for cytochalasin B binding increases in a saturable fashion with [So]. These observations are compared with the predictions of the one-site, alternating conformer model and the two-site model for substrate binding to the sugar transporter, X. The experimental results are inconsistent with the one-site model but are explained by a two-site model in which the ternary complexes of So . X . Si or So . X . CCBi exist and where the binding sites for So and Si display negative cooperativity when occupied by nontransported substrate and little or no cooperativity when occupied by the transported species, D-glucose.

Binding Sites↗
PubMed1978

Kinetic analyses of the sugar phosphate:sugar transphosphorylation reaction catalyzed by the glucose enzyme II complex of the bacterial phosphotransferase system.

The sugar phosphate:sugar transphosphorylation reaction catalyzed by the glucose Enzyme II complex of the phosphotransferase system has been analyzed kinetically. Initial rates of phosphoryl transfer from glucose-6-P to methyl alpha-glucopyranoside were determined with butanol/urea-extracted membranes from Salmonella typhimurium strains. The kinetic mechanism was shown to be Bi-Bi Sequential, indicating that the Enzyme II possesses nonoverlapping binding sites for sugar and sugar phosphate. Binding of the two substrates appears to occur in a positively cooperative fashion. A mutant with a defective glucose Enzyme II was isolated which transported methyl alpha-glucoside and glucose with reduced maximal velocities and higher Km values. In vitro kinetic studies of the transphosphorylation reaction catalyzed by the mutant enzyme showed a decrease in maximal velocity and increases in the Km values for both the sugar and sugar phosphate substrates. These results are consistent with the conclusion that a single Enzyme II complex catalyzes both transport and transphosphorylation of its sugar substrates.

Biological Transport↗
PubMed2006

Synthesis of new amino sugar derivatives from keto-sugars of D-xylose.

Several amino sugars and imino sugar derivatives were synthesized from keto-sugars of D-xylose through a series of reactions such as the Henry reaction, hydrogenation reactions, and nucleophilic addition reactions or substitution reactions. Thiazine derivative 15 was obtained by the reaction of the keto-sugar with NH(2)CSNH(2). Higher carbon sugar 16 was accidentally prepared at room temperature from the keto-sugar in the presence of NH(2)CONH(2). The structures of the compounds were confirmed by spectral analysis. The absolute configurations of all asymmetric carbon atoms of 6 and 8 were confirmed by X-ray crystallographic analysis.

Amino Sugars↗
PubMed1999

Simultaneous determination by capillary gas chromatography of organic acids, sugars, and sugar alcohols in plant tissue extracts as their trimethylsilyl derivatives.

A capillary gas chromatographic (GC) method for the simultaneous determination of organic acids, sugars, and sugar alcohols extracted from plant tissues is described. Plant leaves were extracted in 5% (w/v) perchloric acid and neutralized extracts were purified using C18 cartridges. Organic acids, sugars, and sugar alcohols in purified extracts were converted to their trimethylsilyl (TMS)/TMS-oxime derivatives prior to separation and detection by capillary GC with flame ionization detection (FID). Derivatization procedures were investigated in detail and the compounds of interest were readily converted to their TMS/TMS-oxime derivatives using hexamethyldisiazane reagent in acetonitrile solvent (1:6 v/v) at 100 degreesC for 60 min. The derivatives were sufficiently volatile and stable. The FID response to derivatized compounds was generally linear in the concentration range 30-300 microg ml-1, with detection limits in the order of 3-76 ng. The proposed method was demonstrated for the determination of organic acids, sugars, and sugar alcohols in leaf extracts of two native Australian plants.

Biochemistry↗
PubMed1997

The phosphoenolpyruvate:sugar phosphotransferase system of oral streptococci and its role in the control of sugar metabolism.

Oral streptococci are sugar-fermentative bacteria comprising at least 19 distinct species and are a significant proportion of the normal microbial population of the mouth and upper respiratory tract of humans. These streptococci transport several sugars by the phosphoenolpyruvate:sugar phosphotransferase system (PTS) which concomitantly catalyzes the phosphorylation and translocation of mono- and disaccharides via a chain of enzymic reactions that transfer a phosphate group from phosphoenolpyruvate to the incoming sugar. A number of PTS components, including HPr, Enzyme I and some Enzymes II, have been studied at the biochemical and/or genetical level in Streptococcus salivarius, Streptococcus mutans and Streptococcus sobrinus. Moreover, compelling evidence indicates that the oral streptococcal PTS is involved in the regulation of sugar metabolism. Results are accumulating suggesting that a protein called IIABMan, as well as the phosphocarrier protein HPr, are key regulatory components that allow these bacteria to select rapidly metabolizable sugars, such as glucose or fructose, over less readily utilizable carbohydrates. Circumstantial evidence suggests that the molecular mechanisms by which oral streptococcal PTS exert their regulatory functions differ from mechanisms in other Gram-negative or Gram-positive bacteria.

Bacterial Proteins↗
PubMed1987

The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA.

The mannose permease of the bacterial phosphotransferase system mediates sugar transport across the cytoplasmic membrane concomitant with sugar phosphorylation. It also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA. The permease consists of three different subunits, IIIMan, II-PMan, and II-MMan, which are encoded in a single transcriptional unit ptsLPM. The complete amino acid sequence of the subunits is deduced from the nucleotide sequence. IIIMan (35 kDa) is a hydrophilic protein which is transiently phosphorylated and most likely contains the active site for sugar phosphorylation. II-PMan (28 kDa) is very hydrophobic; II-MMan (31 kDa) is moderately hydrophobic. Both are integral membrane proteins and most likely form the transmembrane channel. All three subunits are required for sugar transport and phosphorylation; II-PMan and II-MMan alone are sufficient for penetration of lambda DNA. Truncated forms of II-MMan and II-PMan are described that mediate lambda DNA penetration but have no apparent sugar transport activity. Residual sugar phosphorylation activity is found with the truncated form of II-PMan. No obvious homologies at the level of amino acid sequence could be detected with other bacterial transport proteins.

Amino Acid Sequence↗
PubMed1986

Glycolipid transfer protein from pig brain transfers glycolipids with beta-linked sugars but not with alpha-linked sugars at the sugar-lipid linkage.

The glycolipid transfer protein purified from pig brain facilitates the transfer of various glycosphingolipids and glyceroglycolipids (Yamada, K., Abe, A. and Sasaki, T. (1985) J. Biol. Chem. 260, 4615-4621). In this paper, the transfer of Man beta 1----4Glc beta 1-Cer and Man alpha 1----4Man beta 1-Cer isolated from a bivalve, Corbicula japonica, the transfer of 3-[Glc alpha 1-]-sn-1,2-diacylglycerol and 3-[Glc alpha 1----2Glc alpha 1-]-sn-1,2-diacylglycerol prepared from Streptococcus lactis, and the transfer of 3-[Glc beta 1-]-rac-1,2-dipalmitylglycerol have been investigated. The transfer of these lipids from liposomes to mitochondria was assayed by the decrease of these lipids in the donor liposomes. These lipids were determined by chromatographic isolation of the lipids, acid hydrolysis of the isolated lipids, and subsequent determination of glucose in the hydrolysate. The glycolipid transfer protein facilitated the transfer of ManGlcCer and ManManGlcCer. The transfer protein did not facilitate the transfer of Glc alpha-diacylglycerol or Glc alpha Glc alpha-diacylglycerol. However, the transfer of Glc beta-dipalmitylglycerol was facilitated by the protein. These results strongly suggest that the glycolipid transfer protein has the specificity to the presence of beta-linked glucose or galactose directly linked to either ceramide or diacylglycerol.

Amino Acid Sequence↗