Characterization of a new oligosaccharide containing myo-inositol found in pregnancy urine.
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Chromatography, Gel↗
Biomedical subjects
M Lhermitte
Publications and source records attributed to M Lhermitte.
Isolation and characterisation of neutral oligosaccharides from human bronchial glycoproteins.
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Bronchi↗
Primary-structure determination of fourteen neutral oligosaccharides derived from bronchial-mucus glycoproteins of patients suffering from cystic fibrosis, employing 500-MHz 1H-NMR spectroscopy.
The structure of carbohydrate units of bronchial-mucus glycoproteins obtained from cystic fibrosis patients was investigated by 500-MHz 1H-NMR spectroscopy and methylation analysis. To that purpose, the mucin was subjected to alkaline borohydride degradation. Neutral oligosaccharide-alditols, ranging in size from disaccharides to pentasaccharides, were isolated. Eight compounds could be purified to homogeneity; furthermore, three fractions were obtained consisting mainly of two components. For all 14 compounds the primary structure could be elucidated. 500-MHz 1H-NMR spectroscopy was found to be effective in detecting heterogeneity and to be invaluable for the determination of structures in mixtures of oligosaccharide-alditols. The structures can be divided into two groups depending on the core disaccharide. One group contains Gal(beta 1 leads to 3)GalNAc-ol as common structural element, the other GlcNAc(beta 1 leads to 3)GalNAc-ol. Both disaccharides were identified as such; the other compounds can be conceived as extensions thereof. The most complex representatives of the two groups are: (formula; see text) The italicized structural elements, comprising the SSEA-1 determinant and the type-1 blood-group-H determinant, are novel sequences in oligosaccharide chains of mucin-type glycoproteins.
Chemical Phenomena↗
Use of lectins for detection of glycoconjugates in the glandular cells of the human bronchial mucosa.
Paraffin-embedded human bronchial biopsies, obtained in macroscopically healthy areas, were examined using nine peroxidase-bound lectins. These were either isolated or purified by affinity column chromatography (Ulex europeus, Triticum vulgare, Glycine max, and Arachis hypogatea lectins) or commercial preparations (Lotus tetragonolobus, Canavalia ensiformis, Helix pomatia, Phaseolus vulgaris, and Lens culinaris lectins) and conjugated to peroxidase (except for concanavalin A). These labeled lectins were used as specific molecular probes to localize differences in carbohydrate-containing components present in the different types of glandular cells of human bronchial mucosa. The choice of fixative was crucial and tests used for this study have shown that Carnoy's solution seems to be the most appropriate solution to preserve mucous glycoproteins in situ. Comparison of the affinity of several lectins for human bronchial glycoproteins and for bronchial mucosa demonstrates the predominance of serum-type glycoproteins in serous cells of the submucosal glands and mucin-type glycoproteins in mucous cells of the submucosal glands and in goblet cells of the bronchial epithelium. Furthermore the data obtained with some lectins, such as Helix pomatia agglutinin, suggest that there are some differences in the mucins synthesized by goblet cells and by mucous cells.
Bronchi↗
Evidence for the presence of the trimannosyl-di-N-acetylchitobiose core in the carbohydrate chains of human-parotid, proline-rich glycoprotein.
The carbohydrate chains of the human-parotid, proline-rich glycoprotein are linked through a single type of carbohydrate-peptide linkage (asparaginyl-N-acetylglucosamine). The structure of the internal part of the carbohydrate chains, determined by chemical, enzymic, and g.l.c.--m.s. methods, includes the trimannosyl-di-N-acetylchitobiose core involved in the carbohydrate-peptide linkage. Furthermore, an L-fucose residue is linked to the 2-acetamido-2-deoxy-D-glucosyl residue linked to the L-asparaginyl residue. The sequence of the peripheral part of the chains has also been determined as alpha-L-Fuc rho leads to beta-D-Gal rho leads to beta-D-Glc rho NAc leads to alpha-D-Man rho, suggesting a double-branched, basic carbohydrate structure.
Glucans↗
Comparative action of reducing agents on fibrillar human bronchial mucus under dissociating and non-dissociating conditions.
Gel=like or fibrillar human bronchial mucus was reduced with mercaptoethanol under dissociating and non-dissociating conditions. Bronchial mucus was solubilized in both conditions; but reduction in phosphate buffer induced more extensive depolymerization of mucus glycoproteins than obtained under reduction in guanidine. Moreover, mucins prepared by reduction in non-dissociating conditions contained less amino acid and more carbohydrate. These data strongly suggest that reduction under non-dissociating conditions does not act only on disulfide bridges but also induces the activation of a mucolytic enzymatic system. They also would explain some of the discrepancies observed in the molecular weight determination and chemical composition of human bronchial mucus glycoproteins purified after reduction of gel-like mucus under different conditions.
Bronchi↗
Oligosaccharides of human bronchial glycoproteins. Neutral di- and trisaccharides isolated from a patient suffering from chronic bronchitis.
Human bronchial glycoproteins from a patient suffering from chronic bronchitis were subjected to alkaline borohydride degradation and a heterogeneous mixture of reduced oligosaccharides and glycopeptides was obtained. The shortest neutral oligosaccharides were subsequently fractionated by DAX4 anion exchange chromatography into 12 fractions. Five major oligosaccharides were purified by preparative paper chromatography. Their structures were determined by using periodic oxidation, methylation analysis, gas liquid chromatography-mass spectrometry, and enzymatic degradation. Two oligosaccharides and three trisaccharides were characterized as galactose (Gal) beta 1 leads to 3 N-acetylgalactosaminitol (GalNActitol), N-acetylglucosamine (GlcNAc) beta 1 leads to 3 GalNActitol, Gal 1 leads to 4 GlcNAc 1 leads to 3 GalNActitol, GlcNAc 1 leads to 3 Gal 1 leads to 3 GalNActitol and fucose alpha 1 leads to 2 Gal beta 1 leads to 3 GalNActitol.
Bronchi↗
Chemical and physical properties of human bronchial mucus glycoproteins.
Human bronchial mucus glycoproteins of different chemical types were isolated by Ecteola and gel exclusion chromatography. Chemical analysis indicated polydispersity with regard to content of sulfate and sialic acid. No blood group A, B or H activity was found in these glycoproteins. Compositions are reported for amino acid and sugar residues for several fractions obtained from both cystic fibrotic and chronic bronchitic mucus. It is noteworthy that glycoproteins extracted from a single subject contain molecules with different acid groups as well as significant differences in carbohydrate chain length.
Amino Acids↗
[Human bronchial mucin glycoproteins prepared from washings of macroscopically healthy bronchi].
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Adult↗
Affinity of bronchial secretion glycoproteins and cells of human bronchial mucosa for Ricinus communis lectins.
The coupling of Ricinus communis lectins to Sephadex G 25 was used in order to study mucins and other glycoproteins from human bronchial secretion. The major part of human bronchial mucins and other glycoproteins such as immunoglobulins A, bronchotransferrin and alpha1-antichymotrypsin were isolated by this procedure. A parallel study of human bronchial mucosa was achieved with peroxidase labeled Ricinus communis lectins; this study characterized goblet cells and mucous cells which contain mucins, and serous cells which are involved in the synthesis or the secretion of the other glycoproteins.
Amino Acids↗
Limulus polyphemus lectin sites in human bronchial mucosa.
The lectin from Limulus polyphemus (limulin) has an affinity for glycoproteins containing N-glycolyl or N-acetylneuraminic residues. By using a peroxidase labeled limulin on human bronchial mucosa sections, it has been possible to demonstrate selectively a diffuse staining within the apical part of the epithelial goblet cells. Whereas, in the submucosal glands serous cells, the labeling appears as small granules localized either at the apical pole or in the whole cytoplasm. In our experimental conditions the labeled limulin has no affinity for mucous cells that are known to contain sialic acid residues.
Arthropods↗
Properties of human neutral bronchial mucins after modification of the peptide or the carbohydrate moieties.
Trypsin and pronase treatment of purified human neutral bronchial mucins released small fragments from the C-terminal end of these molecules and resulted in slight increases in their sedimentation coefficient presumably reflecting conformational changes. The antigenic determinant of neutral bronchial mucins which appears to be located on this C-terminal fragment is destroyed by pronase or by treatments such as periodate oxidation or galactose oxidase-bromine oxidation which modify the carbohydrate moieties. Thus, both amino acid and carbohydrate residues are involved in the structure of the antigenic determinant.
Amino Acid Sequence↗
[Isolation of bronchial mucins from macroscopically healthy human bronchi].
Acids mucins were isolated from a mixture of bronchial washings carried out on 5 subjects, in macroscopically healthy areas of the bronchial tree. Neutral mucins were absent.
Bronchi↗
[Purification and chemical study of a Collocalia glycoprotein].
A glycoprotein was purified from the aqueous extract of "edible bird's nest" (Collocalia) using free flow preparative electrophoresis and represented the main fraction of Collocalia glycoproteins. This glycoprotein is homogeneous upon agarose electrophoresis and slightly polydisperse upon ultracentrifugation (S So 20w = 3,0). The carbohydrate moiety contains galactose, mannose, glucosamine, galactosamine and sialic acid, which is completely released by Clostridium perfringens or Diplococcus pneumoniae neuraminidases and has the same chromatographic behaviour as N-acetyl-neuraminic acid. The peptide part of the glycoprotein is rich in serine, threonine and proline. About 40 p. cent of the hydroxyaminoacids are involved in carbohydrate-peptide linkages.
Amino Acids↗
Isolation and immunological properties of neutral bronchial mucins from a patient with chronic bronchitis.
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Amino Acid Sequence↗
HPLC of oligosaccharides in glycobiology.
Carbohydrate chains of glycoproteins are extremely varied and are a wide variety of different biological processes. Determination of their structures is therefore of great interest in both research and clinical fields. HPLC has proved to be the ideal tool for mono- and oligosaccharide purification and analysis. A wide range of adsorbent and solvent systems are available and we describe in this mini-review the main methods used for the separation and detection of oligosaccharides.
Chromatography, Gel↗
Determination of chloral hydrate and its metabolites (trichloroethanol and trichloracetic acid) in human plasma and urine using electron capture gas chromatography.
Capillary gas chromatography with electron capture detection is described for the quantification of chloral hydrate (CH) and is metabolites trichloroethanol (TCE) and trichloroacetic acid (TCA) in 0.1-1 mL of plasma samples. The method, with 2,2'-dichloroethanol (DCE) as internal standard, involved extraction of chloral hydrate and trichloroethanol with diethyl ether and methylation of trichloroacetic acid with 3-methyl-1-tolyltriazene (MTT), followed by diethyl ether extraction. The method has a detection limit of 5 ng/mL for CH and TCE and 10 ng/mL for TCA and also allows the determination of TCE-glucuronide in 0.1-1 mL of plasma samples. It exhibits good linearity and precision. The method was applied to samples of plasma from a neonate after a single dose of 40 mg/kg of chloral hydrate and from an adult after a single dose of 6.25 mg/kg.
Chloral Hydrate↗
Acid metabolite of progabide pharmacokinetics following single administration in the rabbit with special references to HPLC and (3H) muscimol radioreceptor assay.
The aim of the present study was to monitor plasma levels of progabide and its metabolites in the rabbit following single oral administration of 20 mg.kg-1. The plasma levels were determined selectively using high performance liquid chromatography (HPLC) and then correlated with a global estimation by a (3H) muscimol radioreceptor assay (RRA). In our "in vitro" binding conditions progabide itself was virtually ineffective (IC50 greater than 100 microM) so only RRA active materiel plasma concentrations were studied. A good enough correlation (r = 0.71) has been established between HPLC and RRA plasma concentrations from 0 to 3 hours following oral administration specially considering the absorption phase. But with closed regards to the elimination pharmacokinetic parameters specially the elimination half-life values (t1/2el (RRA) = 1.67 h and t1/2el (HPLC) = 0.70 h) that correlation should be weaker than the former instead metabolites including GABAmide and GABA itself are probably present in amounts likely to affect the displacement of specific binding in the (3H) muscimol radioreceptor assay.
Animals↗