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PubMedDate not supplied

[The identification of fungi by their cellular monosaccharides using gas-liquid chromatography].

The qualitative composition and percent ratio of monosugars in the cell biomass of 101 strains of 5 Candida species and 7 strains of Torulopsis species were determined. It was shown that the major carbohydrate components of the cell biomass of all the Candida species were arabinitol, mannose, fructose, galactose, glucose, sugar alcohol (mannitol) and myoisonitol. C. albicans and C. tropicalis had the highest levels of arabinitol. C. krusei, C. kefyr and T. glabrata contained only traces of arabinitol. The results of the studies indicated that the level of arabinitol could be an additional criterion for the identification of the fungi. A certain relationship between the arabinitol level and the virulence factor was observed which could be confirmed only by parallel investigations on experimental animals.

Candida↗
PubMed1975

[The metabolism of monosaccharides and polyoles].

The metabolism and the various metabolic effects of the sugar substitutes fructose, sorbitol and xylitol have been studied and compared to those of glucose. Fructose, sorbitol, and xylitol were found to be metabolized almost completely in the liver, whereas glucose was metabolized only 20-30% by this organ. The sugars and polyols exhibit a number of common effects characteristic of carbohydrate metabolism. Some of them are for example increase in lactate concentration, increase in lactate-pyruvate ratio, decrease in the concentration of free fatty acids, and decrease in phosphate concentration. The only effect that is restricted to fructose, sorbitol, and xylitol, is the stimulation of uric acid biosynthesis. Though sugar substitutes may be regarded as precursors of glucose, they have only little effect on the increase of blood glucose concentration in normal subjects. This may be due to the glucose - fatty acid cycle. It is to be expected that the use of fructose, sorbitol, and xylitol in diabetes mellitus and under stress situations has certain advantages over glucose.

Blood Glucose↗
PubMed1993

Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin, and lentil (Lens culinaris) lectin.

Titration calorimetry measurements of the binding of methyl alpha-D-mannopyranoside (Me alpha Man), D-mannopyranoside (Man), methyl alpha-D-glucopyranoside (Me alpha Glu), and D-glucopyranoside (Glu) to concanavalin A (Con A), pea lectin, and lentil lectin were performed at 281 and 292 K in 0.01 M dimethylglutaric acid-NaOH buffer (pH 6.9) containing 0.15 M NaCl and Mn+2 and Ca+2 ions. The site binding enthalpies, delta H, are the same at both temperatures and range from -28.4 +/- 0.9 (Me alpha Man) to -16.6 +/- 0.5 kJ mol-1 (Glu) for Con A, from -26.2 +/- 1.1 (Me alpha Man) to -12.8 +/- 0.4 kJ mol-1 (Me alpha Glu) for pea lectin, and from -16.6 +/- 0.7 (Me alpha Man) to -8.0 +/- 0.2 kJ mol-1 (Me alpha Glu) for lentil lectin. The site binding constants range from 17 +/- 1 x 10(3) M-1 (Me alpha Man to Con A at 281.2 K) to 230 +/- 20 M-1 (Glu to lentil lectin at 292.6 K) and exhibit high specificity for Con A where they are in the Me alpha Man:Man:Me alpha Glu:Glu ratio of 21:4:5:1, while the corresponding ratio is 5:2:1.5:1 for pea lectin and 4:2:2:1 for lentil lectin. The higher specificity for Con A indicates more interactions between the amino acid residues at the binding site and the carbohydrate ligand than for the pea and lentil lectin-carbohydrate complexes. The carbohydrate-lectin binding results exhibit enthalpy-entropy compensation in that delta Hb (kJ mol-1) = -1.67 +/- 0.06 x 10(4) + (1.30 +/- 0.12)T(K) delta Sb (J mol-1K-1). Differential scanning calorimetry measurements on the thermal denaturation of the lectins and their carbohydrate complexes show that the Con A tetramer dissociates into monomers, while the pea and lentil lectin dimers dissociate into two submonomer fragments. At the denaturation temperature, one carbohydrate binds to each monomer of Con A and the pea and lentil lectins. Complexation with the carbohydrate increases the denaturation temperature of the lectin and the magnitude of the increases yield binding constants in agreement with the determinations from titration calorimetry.

Calorimetry↗
PubMedDate not supplied

[The amino acid and monosaccharide composition of the extracellular sialo-specific lectins in bacteria of the genus Bacillus].

Chemical composition of extracellular sialo-specific lectins of Bacillus genus bacteria has been studied. It is shown that these biopolymers are glycoproteins distinguished by the quantitative and qualitative composition of proteins and hydrocarbons. It is established that the given bacteria can synthesize one or two extracellular lectins one of which represents N-asparagine-bound glycoprotein, while another one belongs to O-serine/threonine-bound glycoproteins.

Amino Acids↗
PubMed2000

Analysis of N-acetylated hexosamine monosaccharides by ferrocenyl boronation and tandem electrospray ionization mass spectrometry.

A tandem electrospray mass spectrometric (MS(n)) technique for the analysis of N-acetylated hexose carbohydrates using ferrocene boronate (F(c)Bor) derivatization was developed. The biologically important N-acetyl hexosamines can be readily distinguished utilizing this technique. The analysis is made possible by utilizing the inherent electrochemical properties of the electrospray device to produce oxidized, pre-formed single-electron ferrocenyl ions in a non-aqueous solvent system. The electrospray device was modified using a custom built cell consisting of concentric stainless steel tubes, which produced an enhanced signal for the molecular ion of each analyte species. The MS(2) spectra derived from isomeric populations of ferrocenyl boronic esters of these carbohydrates when generated under the same conditions possessed features unique to each sugar allowing easy differentiation between a number of N-acetyl hexosamine isomers.

Acetylation↗
PubMed1990

Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: fine specificity of the monosaccharide-binding site.

The structure of the methyl-alpha-D-mannopyranoside-LOL I complex has been solved by the molecular replacement method using the refined saccharide-free LOL I coordinates as starting model. The methyl-alpha-D-mannopyranoside-LOL I complex was refined by simulated annealing using the program X-PLOR. The final R-factor value is 0.182 [Fo greater than 1 sigma(Fo)]. The isostructural methyl-alpha-D-glucopyranoside-LOL I complex was refined by X-Ray coupled energy minimization using the methyl-alpha-D-mannopyranoside-LOL I structure as a starting model to an R factor of 0.179 (all data). In both crystal forms, each dimer binds two molecules of sugar in pockets found near the calcium ions. The two saccharide moieties, which are in the C1 chair conformation, establish the same hydrogen bond pattern with the lectin. However, the van der Waals contacts are different between the O2, C2, C6, and O6 atoms of the two molecules and the backbone atoms of residues 208-211. Mannose, due to its axial C2 conformation, encloses the backbone atoms of the protein in a clamplike way. Van der Waals energy calculations suggest that this better complementarity of the mannoside molecule with the lectin could explain its higher affinity for isolectin I.

Binding Sites↗
PubMed1992

Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity.

As part of a strategy to determine the precise role of pea (Pisum sativum) lectin, Psl, in nodulation of pea by Rhizobium leguminosarum, mutations were introduced into the genetic determinant for pea lectin by site-directed mutagenesis using PCR. Introduction of a specific mutation, N125D, into a central area of the sugar-binding site resulted in complete loss of binding of Psl to dextran as well as of mannose/glucose-sensitive haemagglutination activity. As a control, substitution of an adjacent residue, A126V, did not have any detectable influence on sugar-binding activity. Both mutants appeared to represent normal Psl dimers with a molecular mass of about 55 kDa, in which binding of Ca2+ and Mn2+ ions was not affected. These results demonstrate that the NHD2 group of Asn125 is essential in sugar binding by Psl. To our knowledge, Psl N125D is the first mutant legume lectin which is unable to bind sugar residues. This mutant could be useful in the identification of the potential role of the lectin in the recognition of homologous symbionts.

Amino Acid Sequence↗