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PubMed2001

Responses of the ant Lasius niger to various compounds perceived as sweet in humans: a structure-activity relationship study.

A behavioural study on the ant Lasius niger was performed by observing its feeding responses to 85 compounds presented in a two-choice situation (tested compound versus water control or sucrose solution). Among these compounds, only 21 were phagostimulating: six monosaccharides (D-glucose, 6-deoxy-D-glucose, L-galactose, L-fucose, D-fructose, L-sorbose), four derivatives of D-glucose (methyl alpha-D-glucoside, D-gluconolactone and 6-chloro- and 6-fluoro-deoxy-D-glucose), five disaccharides (sucrose, maltose, palatinose, turanose and isomaltose), one polyol glycoside (maltitol), three trisaccharides (melezitose, raffinose and maltotriose) and two polyols (sorbitol and L-iditol). None of the 16 non-carbohydrate non-polyol compounds tested, although perceived as sweet in humans, was found to be active in ants. The molar order of effectiveness of the major naturally occuring compounds (melezitose > sucrose = raffinose > D-glucose > D-fructose = maltose = sorbitol) is basically different from the molar order of their sweetness potency in humans (sucrose > D-fructose > melezitose > maltose > D-glucose = raffinose = sorbitol). On a molar basis melezitose is in L. niger about twice as effective as sucrose or raffinose, while D-glucose and D-fructose are three and four times less effective, respectively, than sucrose or raffinose. From a structure-activity relationship study it was inferred that the active monosaccharides and polyols should interact with the ant receptor through only one type of receptor, through the same binding pocket and the same binding residues, via a six-point interaction. The high effectiveness of melezitose in L. niger mirrors the feeding habits of these ants, which attend homopterans and are heavy feeders on their honeydew, which is very rich in this carbohydrate.

Animals↗
PubMed2005

Cryptococcus taeanensis sp. nov., a new anamorphic basidiomycetous yeast isolated from a salt farm.

Cryptococcus taeanensis, a new anamorphic yeast species originating from a salt farm on the Taean peninsula in Korea, is described. Strain 3-12(T) grew by budding, contained ubiquinone Q-10 and xylose in cell hydrolysates, utilized d-glucuronate and did not ferment D-glucose. A molecular phylogenetic analysis based on the large-subunit rRNA D1/D2 domain and ITS region sequences placed C. taeanensis near Auriculibuller fuscus and Bullera japonica, recently proposed taxa of the Tremellales. However, these species were distinguishable based on standard physiological tests used for yeast identification, with characteristics including the assimilation of L-sorbose, absence of ballistoconidia, no arbutin hydrolysis and no growth in the presence of 0.01 % cycloheximide. The isolate exhibited the typical physiology of the genus Cryptococcus Vuillemin, but its large-subunit rRNA D1/D2 domain sequence was clearly distinct from previously described species in the genus. Therefore, on the basis of these results, Cryptococcus taeanensis sp. nov. is proposed; the type strain is 3-12(T) (=KCTC 17149(T) = CBS 9742(T)).

Antifungal Agents↗
PubMed1969

The use of dietary-restricted rat intestine for active transport studies.

1. The effect of dietary restriction (sufficient to produce a loss of about 32% of initial body weight) on intestinal active transport has been studied in the rat by the use of sacs of everted mid-small intestine. Eight D-sugars, four L-sugars and two D-amino acids were employed.2. Dietary restriction enhanced the normally occurring active transport of D-galactose, 3-O-methyl-D-glucose and D-methionine. In addition, sacs of dietary-restricted small intestine were able to concentrate in the serosal fluid D-fucose, D-xylose and D-histidine, which sacs of normal rat intestine could not do. The final (1 hr) serosal/mucosal concentration ratios produced for these actively transported substances were independent of net water movement.3. Sugars which were not concentrated in the serosal fluid of sacs of fully fed or dietary-restricted intestine were D-arabinose, D-fructose, D-glucosamine, D-mannose, L-arabinose, L-fucose, L-sorbose and L-xylose.4. The characteristics of D-fucose and D-xylose active transport suggest that they are transported by the mechanism which actively transports D-glucose. The comparatively low content of D-glucose in dietary-restricted intestine, compared with fully fed intestine, may be part of the explanation for observable active transport of D-fucose and D-xylose by dietary-restricted sacs.5. Thinning of the intestinal wall is believed not to be the cause of the enhanced active transport found during dietary restriction.6. The results show that dietary-restricted rat small intestine may, at times, be more useful than fully fed rat small intestine in the study of intestinal active transport.

Animals↗
PubMed1973

Further effects of chlorpromazine on the hexose permeability of the human erythrocyte.

1. The effect of chlorpromazine on hexose transfer across the human erythrocyte membrane was investigated by optical and isotopic techniques in intact erythrocytes.2. Chlorpromazine produces two phases of inhibition of glucose exit at 17 degrees C in both types of experiment.3. Glucose exchange flux shows a much smaller decrease in flux rate at the same concentrations of chlorpromazine at 17 degrees C.4. Sorbose and glucose entry at 36 degrees C show a similarly complex inhibition by chlorpromazine. The inhibitor constant (K(i)) for these effects with the two sugars is similar.5. An Arrhenius plot shows that the average energy change for the reaction of the carrier with chlorpromazine is -46 kJ mole(-1) and suggests that a drug-induced conformational change in the carrier may occur.6. These findings require models of hexose permeation to contain separate terms in their kinetics for net and exchange fluxes and the predictions of one such model have been compared with the experimental results.

Biological Transport, Active↗
PubMed1975

An experimental method of identifying and quantifying the active transfer electrogenic component from the diffusive component during sugar absorption measured in vivo.

1. The kinetics of absorption of glucose, galactose and alpha-methyl glucoside have been measured in rat jejunum in vivo using a chemical method and a new electrical technique. 2. Sugar absorption estimated by chemical methods exhibited two components. One component was phlorrhizin-sensitive, saturable and generated electrical potential differences (electrogenic active component) while the other was phlorrhizin-insensitive, non-saturable and did not generate electrical potentials (diffusive component). 3. The diffusive component of the actively transported sugars was indentical to the absorption behaviour of sorbose, a hexose that is not actively transferred. 4. A method for correcting the data obtained from chemical absorption studies for the diffusive component was developed. The corrected, operational kinetic constants for 'apparent Km' obtained by this method were not significantly different to values obtained electrically. The identity between the values obtained by both methods supports the concept that they represent a measure of the same rate-limiting step in the absorption process. 5. The application and significance of the techniques is discussed in relation to the clinical assessment of intestinal sugar absorption.

Animals↗
PubMed1973

Facilitated diffusion of monosaccharides in Saccharomyces cerevisiae: experimental investigation of kinetic parameters without the assumptions of symmetry.

Until the question of symmetry or asymmetry in the facilitated diffusion of monosaccharides by Saccharomyces cerevisiae is resolved, attempts to study the transport process cannot be based on assumptions of symmetry, such as equal concentrations at equilibrium or kinetic parameters that are equal in opposite directions. The assumptions of symmetry may be circumvented by measuring efflux against water and against various external concentrations of sugar. The measurement of efflux against water eliminates any involvement of influx, and the separate determinations of influx and efflux parameters do not require that the parameters be equal. Furthermore, the use of relative internal concentrations eliminates any necessity of assuming that the equilibrium concentrations are equal. Since the influx and efflux parameters are to be compared, the measurement of influx on effluxing cells allows both sets of parameters to be determined on cells which are physiologically the same. This procedure has been tested by obtaining the kinetic parameters of l-sorbose transport. The validity of these parameters was demonstrated by using them to generate theoretical efflux curves that fit the experimental data and by showing that they give the best fit curve to the relationship of velocity and permeant concentration. Although the question of symmetry remains unanswered, this procedure has opened the way for experimental evaluation of the situation and further investigation of the transport process in yeast.

Biological Transport↗
PubMed1968

Relationship between sugar structure and competition for the sugar transport system in Bakers' yeast.

Twenty-five sugars have been compared as inhibitors of l-sorbose or d-xylose transport by the constitutive, monosaccharide transport system in bakers' yeast. d-Glucose showed the highest activity (i.e., apparent K(i) = 5 mm). Since all sugars except 2-deoxyglucose showed a decrease in activity relative to glucose (i.e., apparent K(i) = 25 - >2,000 mm), an attempt was made to relate the activity of each sugar with the way its structure differs from that of d-glucose. Assuming that the inhibition was the result of sugar-carrier complex formation, the analysis showed that the transport system has a rather broad specificity for pyranoses. Single changes at each of the five carbons of d-glucose (except for the 2-deoxy derivative) result in variable decreases in activity depending upon the carbon number and the alteration. The largest decrease in activity effected by a single change is the methylation or glucosylation of the anomeric hydroxyl. The combination of two or more changes leads to a decrease which is greater than the decrease in activity resulting from the individual changes occurring alone.

Arabinose↗
PubMed1968

Inhibition by methylphenidate of transport across the yeast cell membrane.

The influence of methylphenidate on glycolysis in yeast cells was studied to describe more fully the nature of the reactions in which this drug participates. CO(2) production and O(2) uptake of yeast cells was inhibited 75% by a 10 mm concentration of the compound. This effect, with glucose as a substrate, occurred at pH 7.0, but not at pH 4.5. Kinetic data indicated that the reaction was noncompetitive and complex; the methylphenidate effect on CO(2) production could not readily be reversed. Glycolysis by cell-free extracts was not inhibited at the 10-mm concentration, but was affected at 100 mm. Utilization of O(2) with maltose and ethyl alcohol as substrates also was reduced. Entry into the cells of a number of different carbohydrates and of glycine was inhibited to different degrees. The loss from suspended cells of materials absorbing at 280 nm was reduced, and the efflux of sorbose, arabinose, and lactose was decreased. Thus, transport into and out of the cells was inhibited and leakage, or permeability, was reduced. It is hypothesized that methylphenidate reacts with a cell membrane constituent, or constituents, and inhibits glycolysis by blocking sugar passage.

Arabinose↗
PubMed1975

Presumptive speciation of Streptococcus bovis and other group D streptococci from human sources by using arginine and pyruvate tests.

A simplified method for speciation of group D streptococci is described. A total of 4,156 streptococcal isolates from human clinical material was tested for ability to hydrolyze esculin in the presence of 40% bile, ferment pyruvate, hydrolyze arginine, and grow in media containing 40% bile or 6.5% NaCl. Streptococci which hydrolyzed esculin in 40% bile, but which did not hydrolyze arginine, were also tested for their ability to ferment raffinose or sorbose. Sixty percent (2,503) of the isolates hydrolyzed esculin in the presence of 40% bile and were thus presumptively identified as group D. By application of the other criteria, 84% of these were speciated as Streptococcus faecalis, 7% were speciated as S. faecium, 6% were speciated as S. bovis, 2% were speciated as S. avium, and 1% were not identified. This scheme was shown to be both reliable and practical for use in the diagnostic laboratory. S. avium and S. bovis isolates were characterized, and 18 S. bovis isolates from patients with bacterial endocarditis were compared physiologically with 151 isolates of this species from other sources.

Arginine↗
PubMed2002

Main polyol dehydrogenase of Gluconobacter suboxydans IFO 3255, membrane-bound D-sorbitol dehydrogenase, that needs product of upstream gene, sldB, for activity.

The D-sorbitol dehydrogenase gene, sldA, and an upstream gene, sldB, encoding a hydrophobic polypeptide, SldB, of Gluconobacter suboxydans IFO 3255 were disrupted in a check of their biological functions. The bacterial cells with the sldA gene disrupted did not produce L-sorbose by oxidation of D-sorbitol in resting-cell reactions at pHs 4.5 and 7.0, indicating that the dehydrogenase was the main D-sorbitol-oxidizing enzyme in this bacterium. The cells did not produce D-fructose from D-mannitol or dihydroxyacetone from glycerol. The disruption of the sldB gene resulted in undetectable oxidation of D-sorbitol, D-mannitol, or glycerol, although the cells produced the dehydrogenase. The cells with the sldB gene disrupted produced more of what might be signal-unprocessed SldA than the wild-type cells did. SldB may be a chaperone-like component that assists signal processing and folding of the SldA polypeptide to form active D-sorbitol dehydrogenase.

Base Sequence↗
PubMed2003

Purification, characterization, and molecular cloning of a pyranose oxidase from the fruit body of the basidiomycete, Tricholoma matsutake.

A new H(2)O(2)-generating pyranose oxidase was purified as a strong antifungal protein from an arbuscular mycorrhizal fungus, Tricholoma matsutake. The protein showed a molecular mass of 250 kDa in gel filtration, and probably consisted of four identical 62 kDa subunits. The protein contained flavin moiety and it oxidized D-glucose at position C-2. H(2)O(2) and D-glucosone produced by the pyranose oxidase reaction showed antifungal activity, suggesting these compounds were the molecular basis of the antifungal property. The V(max), K(m), and k(cat) for D-glucose were calculated to be 26.6 U/mg protein, 1.28 mM, and 111/s, respectively. The enzyme was optimally active at pH 7.5 to 8.0 and at 50 degrees C. The preferred substrate was D-glucose, but 1,5-anhydro-D-glucitol, L-sorbose, and D-xylose were also oxidized at a moderate level. The cDNA encodes a protein consisting of 564 amino acids, showing 35.1% identity to Coriolus versicolor pyranose oxidase. The recombinant protein was used for raising the antibody.

Amino Acid Sequence↗
PubMed2005

The embryo lethality of Escherichia coli isolates and its relationship to various in vitro attributes.

Based on the hypothesis that bacteria with minimal embryo lethality might be good candidates for vertical transmission, 103 lactose-positive Escherichia coli isolates were collected from different broiler-related conditions (sources) and analyzed using a variety of in vitro assays: biochemical profiles, sensitivity to antimicrobials, and the presence of plasmids in the 2000- to 16,000-base pair range. The results of these assays were analyzed to determine if they were associated with, or could be used as predictors of, the degree of lethality these isolates produced in 12-day-old embryos. In addition, the in vitro assay results were analyzed to determine if there was any correlation between any particular pair of factors. On the basis of biochemical profiles, the isolates were classified into 17 different groups; however, only a limited number of biochemical reactions separated a majority of the isolates. The isolates varied considerably in the number and size of plasmids they contained and in their sensitivity to the antimicrobials evaluated. The isolates also varied in their ability to kill chicken embryos--killing from 0% to 100% of those inoculated--yet significant differences were detected in lethality based on source and biochemical profile of the isolate. In addition, a predictive model for embryo lethality was constructed and evaluated based on three characteristics of these 103 isolates, namely, their ability to ferment raffinose and sorbose and their sensitivity to gentamicin.

Analysis of Variance↗
PubMed1991

In vitro inhibition of stable 1,3-beta-D-glucan synthase activity from Neurospora crassa.

Glucan synthase activity of Neurospora crassa was isolated by treatment of protoplast lysates with 0.1% 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate and 0.5% octylglucoside in 25 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid buffer, pH 7.4, containing 5 mM EDTA, 1 mM phenylmethylsulfonylfluoride, 200 mM inorganic phosphate, 10 microM GTP, 1 mM DTT, 10 mM sodium fluoride, and 600 mM glycerol. Resulting activity was partially purified by sucrose gradient density sedimentation. Approximately 70% of enzyme activity in the sucrose gradient peak fraction was soluble and enzyme activity was purified 7.3-fold. Partially purified enzyme activity had a half-life of several weeks at 4 degrees C, and a Km(app) of 1.66 +/- 0.28 mM. Inhibitors (Cilofungin, papulacandin B, aculeacin A, echinocandin B, sorbose and UDP) of 1,3-beta-D-glucan synthase activity were tested against crude particulate and detergent treated enzyme fractions and the Ki(app) of each inhibitor determined. It seems likely that this stable preparation of glucan synthase activity may be useful for in vitro enzyme screens for new glucan synthase inhibitors.

Aminoglycosides↗
PubMedDate not supplied

[Use of NMR spectroscopy in studies of sorbitol and glucose transformation by Gluconobacter oxydans].

NMR spectroscopy was applied for studying the products of glucose and sorbitol oxidation by cells of Gluconobacter oxydans. An analysis of 1H NMR spectra showed that the transformation of glucose results in the formation of diketogluconic acid, and sorbitol is oxidized to sorbose. In the 32P NMR spectra, only a signal of inorganic phosphate was detected, which accumulated in the medium as a result of cell lysis.

Biotransformation↗
PubMed1989

Inhibition of sugar and amino acid transport across rat jejunum by cadmium, copper and mercury.

Cd2+, Cu2+ and Hg2+ (0.5 mM) inhibit the absorption of D-galactose (1 mM) across rat jejunum in vivo. The inhibition increases by 3-5 min previous exposure of the mucosa to the heavy metals, and is appreciably reversed by washing the intestinal lumen with 10 mM EDTA, and in higher proportion with 10 mM dithioerythritol. The metals do not affect the passive absorption of galactose (sugar transport blocked by 0.5 mM phlorizin), or that of L-sorbose. In vitro accumulation of D-galactose by jejunum rings is also inhibited by Cd and Cu. This inhibition is reversed by washing more readily than in vivo. The metals do not affect sugar entry into the tissues in the presence of 0.5 mM phlorizin. The inhibition of the transport component follows a non-competitive kinetics. Cd and Cu inhibit also the L-phenylalanine accumulation by the jejunum rings, but they do not modify the passive entry (in the presence of 40 mM methionine) or that in the absence of Na+. Heavy metals appear to inhibit sugar and amino acid intestinal absorption by their binding to proteins (prevailing to thiol groups) of the luminal membrane of enterocytes, which pertain or are functionally related to the corresponding Na(+)-substrate cotransport system.

Animals↗
PubMed1987

Action of mercury on sugar transport across rat small intestine, in vivo.

Absorption of galactose from in vivo perfused rat jejunum was inhibited by 0.1-0.5 mM Hg2+. A few minutes' delay was required for maximal inhibition values. The effects remained after saline solution washing but were in part reversed by EDTA and in higher proportion by dithioerythritol. Absorption inhibition could be ascribed to impairment of the sugar-Na phlorizin-sensitive cotransport component: The passive apparently diffusional component that remains under 0.5 mM phlorizin and absorption of L-sorbose were unaffected by the metal. Hg action is explained as due to its binding to thiol and perhaps other chemical groups of proteins, at different depths in the membrane, which are directly or indirectly related to the sugar transport system.

Animals↗
PubMed1987

Inhibition of sugar active transport across rat intestine in vivo by cadmium.

Galactose absorption by rat jejunum perfused in vivo is inhibited by 0.5 mM Cd2+. This effect is explained by impairment of the phlorizin-sensitive sugar transport system, as Cd does not modify the absorption of L-sorbose or that of galactose in the presence of 0.5 mM phlorizin. Cd inhibition is observed as early as in the 1st minute, does not increase by previous exposure of the mucosa to the metal and does not decrease after washing with saline solution, but it is entirely reversed by EDTA or dithioerythritol. Results agree with a Cd2+ binding to HS- groups of membrane proteins at the brush border, appertaining or functionally related to the phlorizin-sensitive and Na+ dependent transport system for sugars.

Animals↗