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PubMedDate not supplied

[The role of the carbohydrate composition of the glycocalyx in some species of lactobacilli in the manifestation of their adhesive properties].

Availability of certain monosaccharides in the composition of glycocalyx of lactic acid bacteria (Lactobacillus plantarum--strains 337D and 11/16; Streptococcus thermophilus--strains S1 (nonmucous race) and S5 (mucous race), Enterococcus faecium (K-50) has been investigated with the help of plant lectins with certain carbohydrate specificity labelled by colloid gold. All the microorganisms under investigation were characterized by the presence of N-acetyl-D-galactosamine and N-acetyl-D-glucosamine in rather insignificant amounts. Glycocalyx of lactic acid bacteria was also characterized by availability of essential amount of L-fructose and low amount of sialic acid (except for S. thermophilus S5 (mucous race). Presence of alpha-N-acetyl-D-galactosamine, alpha-D, beta-D-galactose, alpha-D-glucose, alpha-D-mannose in the composition of the lactic acid bacteria glycocalyx composition evidences for the additional role of these monosaccharides in the process of the microorganism adhesion on the human and animal intestine mucosa. It has been confirmed that availability of certain monosaccharides in the composition of surface glycopolymers of lactic acid bacteria was connected with adhesive properties of cells and their existence conditions.

Bacterial Adhesion↗
PubMed1975

Carbohydrate digestion and absorption studies in the horse.

The ability of the horse to digest and absorb soluble carbohydrates was assessed using a series of oral disaccharide tolerance tests followed in the same animals by tolerance tests with the constituent monosaccharides. In horses older than three years, lactose did not produce an increase in the plasma glucose levels but induced the passing of soft faeces, indicating that adult horses are lactose intolerant. Horses of all ages could absorb the glucose: galactose mixture without any change in the faeces. The tolerance is due to a failure to hydrolyse lactose and does not involve the monosaccharide transport systems. These findings correspond to the known development pattern of brush border lactase activity in the equine small intestine. Both sucrose and maltose were rapidly hydrolysed, the resulting tolerance curves closely approximating to those for the constituent monosaccharides. Galactose was absorbed at a similar rate to glucose, although a dose of 1g/kg was necessary to produce galactosaemia. An oral lactose tolerance test (1 g/kg as a 20 per cent solution) could be of clinical value to determine small intestinal mucosal damage in diarrhoeic foals when the continued ingestion of lactose might be detrimental.

Animals↗
PubMedDate not supplied

[Adsorbed receptors for Erwinia carotovor subsp. carotovora macromolecular bacteriocins].

Study of nature of receptors for macromolecular bacteriocins Erwinia carotovora subsp. carotovora has shown that lipopolysaccharide (LPS) of cell membrane is an attaching structure for them. It has been established that enzymic treatment of LPS preparation with its further deproteinization by phenol is necessary for isolation of biologically active lipopolysaccharide. The process of absorption by LPS has been studied quantitatively and it has been shown that it is a low-efficient receptor as compared with LPS included in the native cell membranes. An approach has been proposed for the first time to the estimation of monosaccharide composition of LPS-receptor based on relations between bacteriocin sensitivity and content of monosaccharides. Study of six strains of E. carotovora subsp. carotovora from different sources has shown that the structure of LPS-receptors includes mannose, fucose, xylose, ramnose and two lipophylic monosaccharides of unknown nature. A conclusion has been made that S-LPS (0-chain) is that part which contains the sites of attachment of macromolecular carotovoricins.

Adsorption↗
PubMed1992

Antagonism of lipopolysaccharide-induced priming of human neutrophils by lipid A analogs.

Lipid X, a monosaccharide precursor of the lipid A component of LPS, has been found to antagonize LPS-induced priming of human neutrophils in a manner consistent with competitive inhibition. In this investigation, the inhibition of neutrophil priming by lipid A analogs was found to be specific for LPS-induced priming. Priming of neutrophils by TNF, IL-8, and C5a were all unaffected by increasing concentrations of 3-aza-lipid X-4-phosphate (compound 3), a monosaccharide LPS-antagonist. Unlike lipid X, the pattern of antagonism exhibited by some monosaccharide LPS-antagonists was noncompetitive-like. The relationship between the chemical structure and inhibition pattern was found to be complex and not simply related to the type of acyl linkage at the C-3 position of the glucosamine backbone. Lipid A analogs were found to antagonize calcium ionophore A23187-stimulated leukotriene B4 (LTB4) production from LPS-primed neutrophils in a pattern of inhibition qualitatively similar to that seen with FMLP-stimulated O2- production. Resting and FMLP-stimulated (peak) cytosolic-free calcium levels did not differ significantly between unprimed and LPS-primed neutrophils, (p = 0.67 and p = 0.97, respectively). Furthermore, antagonism of LPS-mediated priming by 3-aza-lipid X-4-phosphate (compound 3) could not be explained by changes in intracellular calcium flux despite marked inhibition of O2- production (p less than 0.0001). Thus, lipid A analogs antagonize only LPS-induced priming and the pattern of inhibition is dependent on the chemical structure. Inhibition of LPS-induced priming by lipid A analogs may involve an early step in the signal transduction pathway common to both O2- and LTB4 generation, but independent of intracellular calcium concentration.

Calcium↗
PubMed1992

O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.

Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera. Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn). However, none of these studies were performed on purified glycoproteins. In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal. Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected. O-linked oligosaccharides were obtained by beta-elimination in the presence of tritiated sodium borohydride. The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities. The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B. The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer). The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase. The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide. The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells. The molecular basis for these alterations awaits further study.

Antibodies, Monoclonal↗
PubMed1997

[High performance liquid chromatographic determination of reducing sugars in fruit juices with laser resonance Raman detection].

A liquid chromatographic method using semi-microcolumn separation combined with laser resonance Raman detection was developed for the determination of monosaccharides in fruit juices. Reducing sugars (galactose, glucose, mannose, arabinose, xylose and ribose) were derivatized with 4-dimethylaminoazobenzene-4'-sulfonyl (DABSYL) hydrazine. The derivatives of the monosaccharides exhibited strong resonance Raman scattering at 1136 cm(-1) when Ar+ laser emission line 488.0 nm was used. A semi-microcolumn Inertsil ODS-2 (250 mm x 1.5 mm i.d.) was used to the separation of the monosaccharide derivatives. The saccharides eluted within 25 min. However the excess DABSYL hydrazine was retained strongly with a retention time of about 60 min. In order to reduce the longer analysis time, the excess DABSYL hydrazine was removed by adding glyoxylic acid and then Na2CO3 aqueous solution when the derivation reaction was finished. As a result, the analysis time was reduced to about a half of its initial run time. The sensitivity of resonance Raman detection greater two orders of magnitude than refractive index (RI) detection. The detection limit of glucose is 10 ng (5.5 pmol). The high selectivity of Raman detection came from the facts that only the interested compounds in a given sample was derived with the Raman labeling reagent and that only the characteristic Raman bands of the derivatives were selectively detected. In this work, in spite of the coexisting large quantities of organic acids in fruit juice, the determined values of glucose agreed well with those obtained by RI detection without any derivatization procedure.

Beverages↗
PubMed1978

Comparative biochemistry of nucleotide-linked sugars.

Nucleotide-linked sugars have 2 general biochemical functions: they are i) intermediates in the formation of monosaccharides found in complex carbohydrates and ii) glycosyl donors of these monosaccharides. Few sugars arise by reactions not involving nucleotide-linked intermediates. Of these few, glucose, mannose, and N-acetylglucosamine are important in that they are transformed after attachment to nucleotides into most other monosaccharides. Several different nucleotides are involved in these transformations. What factor governs the choice of a particular nucleotide carrier for a given reaction is not apparent, but the use of different nucleotides separates pathways of synthesis and offers a means for their independent control by creating reactions unique to the synthesis of certain products and therefore suitable for regulation. Carrying sugars on different nucleotides may also be advantageous by increasing the accuracy of synthesis of complex carbohydrates. For example, a transferase responsible for the transfer of fucose from GDP-fucose is less likely to transfer galactose from UDP-galactose by mistake than galactose from GDP-galactose. The role of nucleotides in the synthesis of complex carbohydrates thus appears related to the specificity of enzymes that catalyze the modification and transfer of nucleotide-linked sugars.

Animals↗
PubMed1986

Specificity of concanavalin A binding to asparagine-linked glycopeptides. A nuclear magnetic relaxation dispersion study.

We have investigated the binding of a series of high affinity asparagine-linked glycopeptides, including high mannose type and a bisected hybrid type, and several related synthetic oligosaccharides, to Ca2+- Mn2+-concanavalin A (ConA), using solvent proton nuclear relaxation dispersion (NMRD) measurements. We find that binding of the glycopeptides induces a common smaller decrease in the NMRD profile of ConA compared to that induced by monosaccharide binding. This effect is also observed with a synthetic analog of complex-type carbohydrates, hepta, which also shows enhanced affinity for the protein relative to monosaccharide binding. The high affinity of the glycopeptides and hepta, and their unique effects on the NMRD profile, are mimicked by binding of the trimannosyl oligosaccharide, 3,6-di-O-(alpha-D-mannopyranosyl)-D-mannose, which is present as a structural element in all of the glycopeptides and synthetic oligosaccharides. However, adding a so-called bisecting N-acetyl-D-glucosamine residue to the trimannosyl oligosaccharide greatly reduces its binding affinity and produces a decrease in the NMRD profile of the protein similar to that observed for monosaccharide binding. These results indicate that the trimannosyl oligosaccharide is a unique moiety recognized by the lectin for high affinity and extended site binding, and the presence of a bisecting N-acetyl-D-glucosamine residue in the trimannosyl oligosaccharide eliminates this type of interaction. The results also demonstrate that ConA primarily binds to the outer trimannosyl regions of high mannose and bisected hybrid-type glycopeptides compared to the central trimannosyl region of complex glycopeptides. Two mechanisms of enhanced affinity binding of saccharides and glycopeptides to ConA are discussed.

Asparagine↗
PubMed1986

Human fibrinogen specifically binds hyaluronic acid.

Fibrin and hyaluronic acid (HA) are macromolecules whose concentrations are elevated at the same time in the extracellular space of damaged tissues. We have investigated whether HA can bind to fibrinogen using solid phase and soluble assays. Purified human fibrinogen specifically bound to HA-Sepharose to a greater extent (greater than 5-fold) than did alpha 1-acid glycoprotein, DNaseI, ovalbumin, haptoglobin, or lysozyme. Fibrinogen did not bind to ethanolamine-Sepharose, a control chromatographic support. Treatment of HA-Sepharose containing bound 125I-fibrinogen with ovine testicular hyaluronidase released 44% of the 125I radioactivity, indicating that fibrinogen was specifically bound to HA. Moreover, 125I-fibrinogen bound to HA-Sepharose could be displaced by free HA but not by either of the monosaccharide components of this polymer, glucuronic acid, or N-acetylglucosamine. Chondroitin sulfate and polygalacturonic acid competed only weakly for bound 125I-fibrinogen. Bound 125I-fibrinogen was also not released by high concentrations of NaCl (up to 4 M), indicating that the interaction is not simply ionic. The apparent affinity of fibrinogen for HA covaried with the molecular weight of the HA. Small HA oligosaccharides (Mr = 3900) were only 50% as effective as larger HA (Mr = 8 X 10(5)) in eluting bound 125I-fibrinogen from HA-Sepharose. The optimal oligosaccharide size for displacement of bound 125I-fibrinogen was greater than or equal to 200 monosaccharides. Additionally, the amount of 125I-fibrinogen bound to HA-Sepharose was directly related to the size of the HA-amine linked to the affinity support. The affinity constant for fibrinogen binding to 125I-HA (approximately 150 monosaccharides) is estimated to be at least 2 X 10(7) M-1. These results demonstrate for the first time a specific, reversible binding between HA and fibrinogen.

Electrophoresis, Polyacrylamide Gel↗
PubMed1986

Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa.

Oligosaccharides (10-20 monosaccharide units) with high affinity for antithrombin, as well as larger high-affinity heparin fractions (having relative molecular masses between 6,000 and 21,500), all markedly accelerated the inhibition of Factor Xa by antithrombin. Moreover, all high-affinity oligosaccharides and heparins enhanced, to a similar extent, the amount of free proteolytically modified antithrombin cleaved at the reactive bond by Factor Xa. In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme. All high-affinity fractions studied had similar affinities for antithrombin, as determined by fluorescence titrations. In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin. Moreover, similar binary complexes with 3H-labeled octadecasaccharide or larger chains, but not with smaller oligosaccharides, were capable of binding to matrix-linked inactivated thrombin. These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units. Similar complex formation apparently is not required for the acceleration of the antithrombin-Factor Xa reaction.

Animals↗
PubMed1986

[Acceptor specificity of mannosyl transferases from Salmonella of serotypes C2 and C3].

Synthetic mono- and disaccharide derivatives of moraprenyl pyrophosphate were studied as mannose acceptors during the assembly of the repeating unit Rha-Man-Man-Gal of the Salmonella newport (serogroup C2) and S. kentucky (serogroup C3) O-antigens. Mannosyl transferases revealed strict specificity towards the configuration of terminal monosaccharide residue at C1 as well as to the type of linkage between monosaccharide residues in the disaccharide acceptor. The specificity of mannosyl transferases towards the structure of subterminal monosaccharide was not absolute. Alpha-D-Glucose and alpha-D-mannose derivatives were found not to serve as mannosyl residue acceptors, whereas those of alpha-D-talose, alpha-D-fucose, 4-deoxy-D-xylo-hexose and Man (alpha 1-3) glucose were substrates in enzymatic mannosylation with formation of polyprenyl pyrophosphate trisaccharides. These derivatives could serve as substrates for two subsequent enzymatic reactions: rhamnosylation and polymerization of the repeating units, yielding 40-60% of the polysaccharides.

Hexosyltransferases↗
PubMed1979

Biosynthesis of yeast glycoproteins. Processing of the oligosaccharides transferred from dolichol derivatives.

The oligosaccharides previously bound to dolichol diphosphate were isolated from Saccharomyces cerevisiae cells incubated with [U-14C]glucose. Five compounds were obtained that migrated with RGlucose of 0.100, 0.120, 0.145, 0.180, and 0.215 on paper chromatography. All of them contained mannose and 2 N-acetylhexosamine residues. The substances that migrated with the three lower RGlucose values had, in addition, glucose units. The structure of the oligosacchardies was very similar if not identical with that of the oligosaccharides isolated from the dolichol diphosphate derivatives synthesized "in vitro" by yeast or rat liver particulate preparations or "in vivo" by dog thyroid or rat liver slices as judged by their migration on paper chromatography, monosaccharide composition, and degradation compounds produced by alpha-mannosidase treatment or acetolysis. The oligosaccharides previously bound to asparagine residues in proteins were isolated from yeast cells which had been pulsed with [U-14C]glucose and chased with medium containing the unlabeled monosaccharide. The samples taken after very short pulses contained four oligosaccharides that migrated with RGlucose of 0.100, 0.120, 0.145, and 0.180 on paper chromatography. The first three compounds contained glucose, mannose, and 2 N-acetylhexosamine residues whereas the one that migrated with a RGlucose of 0.180 was devoid of the former monosaccharide. Samples taken after short chase periods revealed that the compounds that migrated with the lower RGlucose values gradually disappeared and were converted to the oligosaccharide with the higher RGlucose value was they lost their glucose residues. Similar analysis as those mentioned above showed that the structures of these compounds were similar to those of the dolichol diphosphate-bound oligosaccharides. Samples taken after longer chase periods revealed that the oligosaccharide that migrated with a RGlucose of 0.180 was subsequently either enlarged by the addition of more mannose residues or trimmed to smaller sizes.

Carbohydrates↗
PubMed1979

Biosynthesis of proteoglycans and their assembly into aggregates in cultures of chondrocytes from the Swarm rat chondrosarcoma.

Cultured chondrocytes from the Swarm rat chondrosarcoma incorporate [35S]sulfate into proteoglycans typical of hyaline cartilage. The movement of newly synthesized proteoglycans from inside the cells into the extracellular matrix and, finally, into the culture medium was examined by measuring the distribution of 35S-labeled proteoglycans in the medium, a 4 M guanidine HCl extract of the cell layer, and in the remaining residue for a number of chase times following a 5-min pulse with [35S]sulfate. When hyaluronate oligosaccharides containing greater than or equal to 10 monosaccharides were included in the chase media, a proportion of newly synthesized proteoglycans were displaced from the matrix (4 M extract) into the culture medium. This displacement was greatest when oligomers were in the chase media between 10 and 20 min after the pulse, approximately the time when the molecules are being secreted from the cells. The proportion of link-stabilized aggregate in the medium was examined by Sepharose 2B chromatography after adding an excess of unlabeled monomer which displaces labeled monomer from complexes with hyaluronate which are not link-stabilized. The proportion of link-stabilized aggregate increased from 12% to about 70% between 12 and 120 min of chase. The presence of 40 micron hyaluronate oligosaccharides of 16 monosaccharides in the chase media retarded but did not prevent aggregate formation. Oligomers of about 50 monosaccharides, which are large enough to bind both a monomer proteoglycan and a link protein, almost completely prevented the formation of the large link-stabilized aggregates. The results suggest: (a) newly synthesized proteoglycans are not bound into link-stabilized aggregates at the time of secretion; (b) hyaluronic acid oligomers which are long enough to interact only with the hyaluronic acid-binding site of proteoglycans will retard but not prevent link-stabilized aggregation; and (c) hyaluronic acid oligomers long enough to accommodate additionally a link protein form a link-stabilized ternary complex and prevent aggregation with larger hyaluronic acid molecules.

Animals↗
PubMed1977

[Carbohydrate absorption and malabsorption (author's transl)].

Starch is digested intraluminally by alpha-amylase to maltose, maltotriose, and alpha-limit dextrins. These products, as well as the disaccharides sucrose and lactose, undergo enzymatic hydrolysis to monosaccharides at the brush border surface. The monosaccharides enter the absorbing cell by specific transport mechanisms ("carriers"). Primary carbohydrate (CH) intolerance is characterized by the congenital or acquired absence of individual brush border enzymes or of monosaccharide "carriers" without morphologic abnormalities of the intestinal villus: lactose, sucrose and trehalose intolerance and glucose-galactose malabsorption (brush border diseases). Secondary CH intolerance arises when surface digestion and absorption are reduced due to structural changes of the intestinal mucosa: e.g., decrease or absence of villi with sprue and reduction of the absorbing surface with intestinal resection. Watery diarrhea is the lead symptom. Many drugs delay or interfere with CH absorption. This action may be viewed either as an unwanted side effect or as a welcome therapeutic principle.

Carbohydrate Metabolism↗
PubMed1981

Chemical analysis of glycosaminoglycans inhibiting DNA synthesis.

Sulfated glycosaminoglycans having inhibitory activity in cellular and subcellular systems were found in some tumor tissues from humans. These glycosaminoglycans inhibited more efficiently DNA synthesis of virus transformed cells (SV40-WIRL-3 cells) than their parent normal cells (WIRL-3 cells). Sulfated glycosaminoglycans found in normal human and non-tumor tissues did not have as high an inhibitory activity on DNA synthesis by cells used in this investigation as those from some human tumor tissues. The former did not inhibit as effectively DNA synthesis by virus transformed cells, as DNA synthesis by their normal parent cells. The monosaccharide composition of these sulfated glycosaminoglycans showed N-acetyl glucosamine (Glu-NAc) as a main monosaccharide, and xylose (Xyl), glucose (Glu), galactose (Gal), hyaluronic acid (Hu-A) as minor monosaccharides. N-acetyl galactosamine was not detected.

Adult↗
PubMed1978

Biphasic association of p-nitrophenyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside and concanavalin A as detected by stopped flow spectroscopy.

Kinetics of binding of p-nitrophenyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside (M2) to concanaviln A (con A) were examined. The time course of formation of a M2 . con A complex is clearly biphasic, whereas the association with con A of p-nitrophenyl 2-O-methyl-alpha-D-mannopyranoside and other monosaccharides is a monophasic process. The biphasic time course of the binding of M2 to conA is most simply explained in terms of a model wherein the disaccharide can bind to con A two different ways. In the initial rapid phase of the biphasic reaction, both complexes form in amounts determined by the relative values of the rate constants for association. In the subsequent slow phase, the complexes equilibriate according to the relative values of the initial constants for formation of each complex. The enthalpy of activation for formation of the initial complexes with M2 is about 4 kcal/mol less favorable than for monosaccharides, whereas the entropy of activations about 14 e.u. more favorable for binding of the disaccharide. These differences in the activation parameters for binding M2 and monosaccharides suggest that con A interacts simultaneously with groups on both mannopyranosyl residues.

Calorimetry↗
PubMed1997

Epitope mapping of twelve monoclonal antibodies against the phenolic glycolipid-I of M. leprae.

Epitope mapping of 12 monoclonal antibodies (MAbs) directed to the trisaccharide part of the phenolic glycolipid-I (PGL-I) of Mycobacterium leprae was carried out by using the set of chemically synthesized sugar-BSA conjugates. The results can be summarized as follows: mAb (1-21), mAb (1-24) and mAb (1-25) recognized the outer (nonreducing end) monosaccharide of the trisaccharide chain of PGL-I. However, the affinity of these MAbs to the outer monosaccharide was weak. They required the contributions of some parts of the second sugar for enough affinity. MAbs ml 6A12, ml 8A2, ml 8B2, and PG2 B8F recognized the outer disaccharide. MAb F47-21-3 recognized the outer disaccharide and some parts of the third sugar. MAb SF 1 recognized the trisaccharide of PGL-I. MAb 3D1-A9 recognized the phenol group and the structure around the branching point on the carrier protein in addition to the trisaccharide. MAbs DZ 1 and 2G3-A8 had unique characters which recognized the inner part of the sugar chain. MAb DZ 1 recognized the inner (reducing end) disaccharide. MAb 2G3-A8 recognized the inner monosaccharide, phenol group and the structure around the branching point on the carrier protein. All of the MAbs tested, except for ml 6A12, recognized the anomeric configurations in the sugar parts they recognized; ml 6A12 recognized the anomeric configuration only within the outer disaccharide. This set of MAbs, which were well defined on their binding specificity, promises to be an effective tool for the immunological study of PGL-I and the clinical assessment of leprosy.

Antibodies, Bacterial↗
PubMed1992

High-performance anion-exchange chromatography coupled with mass spectrometry for the determination of carbohydrates.

Methodology has been developed to couple high-performance anion-exchange chromatography (HPAE) with mass spectrometry utilizing the ion spray liquid chromatography/mass spectrometry (LC/MS) interface. Anion micro-membrane suppression (AMMS) has been used to remove the high concentrations of NaOH and NaOAc (10-400 mM total [Na+]) necessary for the separation of mixtures of monosaccharides and oligosaccharides. Post-suppressor addition of CH3CN/H2O solutions containing NH4OAc or LiOAc provided low-nanomole detection of the monosaccharides by selected ion monitoring of the cationized adducts. Maltooligosaccharide mixtures (three to seven residues) were separated and detected by the HPAE/AMMS LC/MS system in the full-scan mode. Low declustering potentials (35 V) in the LC/MS API source afforded intact singly and doubly charge ammoniated and diammoniated adducts of the sugars. Higher declustering potentials (65 V) produced abundant fragmentation of the ammoniated adducts. The corresponding lithiated and dilithiated species produced intact molecule ion species at higher declustering potentials. The endo H-released oligomannose species from RNase B were determined by the HPAE/AMMS LC/MS system as ammoniated adducts and resulting fragment ions with a high declustering potential (95 V) in the full-scan mode.

Carbohydrates↗