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Adhesive properties of Bifidobacterium bifidum strain DSM 20082 were studied by the hemagglutination test and an enzyme-linked immunosorbent assay (ELISA). B. bifidum caused agglutination of human A, B, and O erythrocytes and rabbit erythrocytes, but the interactions were not specific of blood group antigens. The hemagglutination was inhibited by porcine gastric mucin and rat intestinal and colonic mucin. B. bidifum was shown to adhere to different immobilized mucosal glycoproteins and to glycophorin A, a specific erythrocyte membrane glycoprotein. The data obtained with many glycosylated components indicated that B. bifidum receptors involved in the hemagglutination test were not the same as those that adhere to mucus glycoproteins. The results suggest that the mucosal preparations contain receptors for specific bacterial adhesins, but their structures remain to be determined. [ABSTRACT FROM AUTHOR]

The authors have determined the complete structure of a hexasaccharide isolated from human milk: the dilactaminyl (or di-N-acetylneuraminyl)-lacto-N-tetraose. This new sugar results from the substitution onto the lacto-N-tetraose (β-D-galactopyrannoside-1,3-β-D-N-acetylglucosaminopyrannosido-1,3-β-D-galactopyrannosido-l,4-D-glucopyrannose) of two residues of N-acetylneuraminic acid. The first is grafted in the 3-position of the terminal galactose residue and the second in the 6-position of the N-acetylglucosamine residue. [ABSTRACT FROM AUTHOR]

Examines the adhesion of bifidobacterial strains to human enterocyte-like cells and binding to mucosal glycoprotein. Existence of adhesion on the apical brush border of cultured cells; Inhibition of bacterial adhesion to cultured cells; Association of the bacterial adhesive with proteinaceous components.

The objective of the present study was to determine the effect of the soluble cytoplasmic fraction from Bifidobacterium bifidum DSM 20082 (Bb) lysate on peripheral blood T cells. In peripheral blood mononuclear cells of healthy subjects, cytotoxic activity, proliferation, apoptosis, and up-regulation of CD8 or CD4 molecules in T cells were examined. When peripheral blood mononuclear cells were stimulated with Bb lysate, the main effect was observed in CD8+ cells as a significant increase of CD8 molecules in a dose-dependent manner, and this behavior was observed at 24, 48, and 72 h after stimulation; in contrast, stimulation with Bb lysate showed no effect on the up-regulation of CD4 molecules in T helper cells. Further Bb lysate did not induce proliferation activity in either CD8+ or CD4+ cells. Bb lysate induced activation of CD8+ cytotoxic activity against autologous monocytes. Around 80% of the cells stimulated with Bb lysate were positive to peanut agglutinin (PNA), suggesting that the stimulated CD8+ cells corresponded to activated/effector cellular populations. When apoptosis was determined, there were no differences between stimulated and non-stimulated cells. Our results indicate that Bb lysate is able to increase cytotoxic activity of peripheral CD8+ cells, without affecting lymphocyte survival.

Bifidobacterium bifidum, in contrast to other bifidobacterial species, is auxotrophic for N-acetylglucosamine. Growth experiments revealed assimilation of radiolabelled N-acetylglucosamine in bacterial cell walls and in acetate, an end-product of central metabolism via the bifidobacterial D: -fructose-6-phosphate shunt. While supplementation with fructose led to reduced N-acetylglucosamine assimilation via the D: -fructose-6-phosphate shunt, no significant difference was observed in levels of radiolabelled N-acetylglucosamine incorporated into cell walls. Considering the central role played by glutamine fructose-6-phosphate transaminase (GlmS) in linking the biosynthetic pathway for N-acetylglucosamine to hexose metabolism, the GlmS of Bifidobacterium was characterized. The genes encoding the putative GlmS of B. longum DSM20219 and B. bifidum DSM20082 were cloned and sequenced. Bioinformatic analyses of the predicted proteins revealed 43% amino acid identity with the Escherichia coli GlmS, with conservation of key amino acids in the catalytic domain. The B. longum GlmS was over-produced as a histidine-tagged fusion protein. The purified C-terminal His-tagged GlmS possessed glutamine fructose-6-phosphate amidotransferase activity as demonstrated by synthesis of glucosamine-6-phosphate from fructose-6-phosphate and glutamine. It also possesses an independent glutaminase activity, converting glutamine to glutamate in the absence of fructose-6-phosphate. This is of interest considering the apparently reduced coding potential in bifidobacteria for enzymes associated with glutamine metabolism.

Purification of the lectin from Phaseolus acutifolius var. escumite was achieved by affinity chromatography on a column containing glutaraldehyzed membranes from blood group O erythrocytes. The lectin is a tetrameric glycoprotein of 121 kDa with 10% of sugar by weight composed by four subunits of 30 kDa as determined by SDS-PAGE. The lectin is composed of four isolectins as determined by ion-exchange chromatography on a mono-S column. The lectin and its isolectins showed identical NH2 terminal residues (ANDLSFNFQR FNETN) with homology to the PHA leucoagglutinin-precursor. Peptide mass fingerprint from each lectin isoform determined from tryptic peptides by MALDI-TOF (matrix assisted laser desorption ionization-time-of-flight) showed differences among subunits, thus suggesting microheterogeneity in their amino acid sequences or different glycosylation patterns. The lectin and its four isolectins agglutinated erythrocytes without serological specificity and showed mitogenic activity on human leukocytes; moreover, the main effect was rather toward CD8+ than to CD4+ human peripheral lymphocytes. The lectin from escumite was not inhibitable by simple sugars; however, the specificity of the lectin and its isoforms was mainly addressed toward galactose residues present in bi- or triantennary N-acetyllactosamine-type glycans.

Neutrophils participate in host protection and central to this process is the regulation of oxidative mechanisms. We purified by affinity chromatography the receptor for the GlcNAc-specific WGA from CD14+ CD16+ cell lysates (WGAr). The receptor is a 141 kDa glycoprotein constituted by two subunits of 78 and 63 kDa. It is mainly composed of Ser, Asx, and Gly, and, in a minor proportion, His, Cys, and Pro. Its glycan portion contains GlcNAc, Gal, and Man; NeuAc and GalNAc were identified in a minor proportion. The amino acid sequence of the WGA receptor was predicted from tryptic peptides by MALDI-TOF, both subunits showed homology with cytokeratin type II (26 and 29% for the 78 and 63 kDa subunits, respectively); the 78 kDa subunit showed also homology with the human transferrin receptor (24%). Antibodies against WGAr induce higher oxidative burst than WGA, determined by NBT reduction; however, this effect was inhibited (p < 0.05) with GlcNAc suggesting that WGAr participates as mediator in signal transduction in neutrophils.

We determined the effect of low molecular weight components (LMWC) from healthy juvenile and adult Macrobrachium rosenbergii hemolymph on lectin activity and oxidative burst (OB) in hemocytes. In an attempt to identify the LMWC that affect the lectin's hemagglutinating activity or oxidative burst, we determined the hemolymph carbohydrates and free amino acids (FAA) concentration. The LMWC (<2000 Da) were obtained after dialysis of the hemolymph. Our results showed that LMWC from juveniles exerted a greater inhibition on lectin than LMWC from adult hemolymph. Production of superoxide radicals by hemocytes was lower in the presence of juvenile (p<0.05) as compared to adult LMWC. FAA composition of the hemolymph and of LMWC from adults showed higher proportion of alanine (which corresponded to 25% of total FAA) and proline (>20%); whereas, in juveniles, the main FAA identified were glycine (>40%) and alanine (26%). N-Acetyl-D-glucosamine (GlcNAc) was the main sugar residue in the hemolymph and LMWC from juveniles; its concentration was 2.4 times higher than glucose (Glc), whereas, in adults, Glc was the main free sugar residue. Our results suggest that the proportion of FAA and carbohydrates in the hemolymph of M. rosenbergii seems to be correlated with the maturation process; furthermore, the high proportion of free GlcNAc and glycine regulate, in the juvenile stage, lectin activity and cellular oxidative mechanisms, respectively.

Amaranthus leucocarpus lectin (ALL) is specific for GalNAc, and recognizes human T cells. The receptor for ALL was purified from T cells using biotin-labeled lectin and avidin-agarose as affinity matrix. It is a 70-kDa glycoprotein, constituted mainly by serine, glycine, and glutamic acid; its glycosidic portion contains mainly GalNAc; galactose, sialic acid, mannose, and GlcNAc were identified at a lower proportion. By ionic strength chromatography, as well as double dimension electrophoresis, we identified four isoforms of the ALL-receptor. N-terminal amino acid was blocked both in the ALL-receptor and its isoforms, therefore, tryptic peptides of ALL-receptor, analyzed through MALDI-TOF, were compared with the relative values obtained from the NCBInr (ProFound 2004/06/01) database. Our results indicated that the tryptic peptides obtained showed 54% homology with a DnaK-core molecular chaperone, 47% with human KIAA protein, and 44% with heat shock protein 8. The most frequent phenotype of the CD4 or CD8 ALL+ T cells was CD45RA+ CD27+; 26% of ALL+ T cells were CD25+ and 13% were CD69+, indicating that the glycoprotein recognized by ALL is present mainly on naive or quiescent T cells.

Although the ability of Bifidobacterium spp. to grow on fructose as a unique carbon source has been demonstrated, the enzyme(s) needed to incorporate fructose into a catabolic pathway has hitherto not been defined. This work demonstrates that intracellular fructose is metabolized via the fructose-6-P phosphoketolase pathway and suggests that a fructokinase (Frk; EC 2.7.1.4) is the enzyme that is necessary and sufficient for the assimilation of fructose into this catabolic route in Bifidobacterium longum. The B. longum A10C fructokinase-encoding gene (frk) was expressed in Escherichia coli from a pET28 vector with an attached N-terminal histidine tag. The expressed enzyme was purified by affinity chromatography on a Co(2+)-based column, and the pH and temperature optima were determined. A biochemical analysis revealed that Frk displays the same affinity for fructose and ATP (Km(fructose) = 0.739 +/- 0.18 mM and Km(ATP) = 0.756 +/- 0.08 mM), is highly specific for D-fructose, and is inhibited by an excess of ATP (>12 mM). It was also found that frk is inducible by fructose and is subject to glucose-mediated repression. Consequently, this work presents the first characterization at the molecular and biochemical level of a fructokinase from a gram-positive bacterium that is highly specific for D-fructose.

Biogenic amine levels and other biochemical indicators were measured to study the safety of and the loss of freshness in iced Atlantic cod. Biogenic amine content exhibited high variability during iced storage of Atlantic cod. Ornithine and lysine decarboxylase activity apparently increased at the end of the storage period. Amino acid activity was probably generated by endogenous amino acid decarboxylases of raw fish. No statistical differences were observed in the total volatile base fraction or in the ammonia or monomethylamine contents during iced storage. However, trimethylamine contents showed a significant exponential relationship with time and sensory score. Cod formed inosine as the major metabolite of IMP. The H and G indices showed a linear relationship with time and sensory score and served as good indicators of cod freshness quality. However, the K, Ki, and P indices showed a logarithmic relationship with time and sensory score. IMP, K, Ki, and P served as indicators of freshness lost during the early stages of chilled storage of cod.

The serum of the freshwater prawn contains a sialic acid specific lectin (MrL) that agglutinates erythrocytes from rat and rabbit, as well as some Gram negative and positive bacterial strains. In this work, we performed the chemical characterization of the MrL purified by affinity chromatography on stroma from rat erythrocytes and by ion exchange chromatography. In its active form, MRL is a dimeric glycoprotein with 9.5 kDa per subunit. The amino acid sequence of the lectin was deduced from peptides obtained after trypsin treatment by matrix-assisted laser desorption ionization mass spectrometry-time of flight analysis (MALDI-TOF). The predicted amino acid sequence of the lectin showed 54% homology with the hyperglycemic hormone from Macrobrachium rosenbergii. It also showed homology with the variable region of the human immunoglobulin kappa (22%) and lambda (27%) light chains. The lectin is a glycoprotein with 11% (w/w) carbohydrate content and is constituted by Gal, Man, GlcNAc, GalNAc and NeuAc in a molar ratio of 4:3:2:1:0.6. The primary structure of the carbohydrate chains of the lectin from the freshwater prawn was determined by affinity chromatography of MrL-glycopeptides on Con A and LCA lectin columns, which indicated that the main carbohydrate chains conforming the lectin are N-glycosidically linked. Man3 GlcNAc2.1 oligosaccharides were the most abundant structures with 57%) followed by Gal1.3 Man3 GlcNAc2.8 with 24%. Our results suggest that the freshwater prawn possess a lectin in the hemolymph plasma, related to those from the immunoglobulin superfamily.

From the serum of juvenile freshwater prawns, we isolated by affinity chromatography on glutaraldehyde-fixed rat erythrocytes stroma, immobilized in Sephadex G-25, a sialic acid specific lectin of 9.6 kDa per subunit. Comparative analysis against adult organisms purified lectin, by chromatofocusing, showed that the lectin from juvenile specimens is composed by four main isoforms with a pI of 4.2, 4.6, 5.1, and 5.6, whereas the lectin from adults is eluted at pH 4.2. The amino acid composition of the lectin obtained from adult and juvenile stages suggest identity, but the compositions are not identical since a higher content of carbohydrates was found in the lectin from younger organisms. The freshwater prawn lectin showed specificity toward N-acetylated amino sugar residues such as GlcNAc, GalNAc, Neu5Ac and Neu5,9Ac; but in juvenile organisms the lectin showed three times less hemagglutinating activity than the lectin from adults. Both lectins agglutinated rat, rabbit and chicken erythrocytes, indicating that Neu5,9Ac in specific O-glycosydically linked glycans seems to be relevant for the interaction of M. rosenbergii lectins with their specific cellular receptor. Our results suggest that the physicochemical characteristics of the lectin from the freshwater prawn are regulated through maturation.

Fish muscle decarboxylases generate biogenic amines during spoilage. We monitored spoilage in plaice and whiting by assaying biogenic amines represented by the amine index (AI), and by using expert assessors to determine a freshness index (FI) for each fish. First we characterized the assessor- and fish species-related effects on FI, and then we sought to correlate changes in AI and FI by statistical data analysis. We propose rejection limits on the basis of our findings.

A new enzyme has been characterized in a cell-free extract of Bifidobacterium bifidum that catalysed the reversible phosphorolytic cleavage of beta-1,3-galacto-oligosaccharides. In the presence of Pi, the phosphorolysis reaction was favoured and was accompanied by a Walden reaction. Cleavage of the beta-glycosidic linkage gave an alpha-galactoside derivative (alpha-D-galactose 1-phosphate). The enzyme possesses a high specificity for beta-D-galactosido-(1, 3)-N-acetylglucosamine and beta-D-galactosido-(1, 3)-N-acetylgalactosamine. This purified intracellular enzyme had an estimated molecular mass of 140 kDa. The galactophosphorolytic activity on disaccharides was optimal at pH 6-6.5 and the reverse reaction was optimal at pH 5.5-6. The temperature optimum for phosphorolysis and the reverse reaction was approx. 50-55 degrees C. This enzyme is of particular interest in degrading some beta-D-Gal(1, 3) linkages and should be classified as EC 2.4.1.-.

The receptor for Amaranthus leucocarpus lectin from CD-1 resident macrophages was purified with affinity chromatography with biotin labeled A. leucocarpus lectin and using avidin-agarose as affinity matrix. The receptor is a glycoprotein of 70 kDa that contains 18% of sugar by weight; it is mainly composed of galactose and N-acetyl-D-galactosamine in its saccharidic portion, and lacks sialic acid; the protein is rich in glycine, serine and alanine and lacks cysteine residues. The amino terminus of the receptor is blocked. By ionic strength chromatography on a mono P column in anionic form we purified three isoforms from the affinity purified receptor, each showing quantitative differences in glycosylation. The A. leucocarpus lectin receptor is identified only in resting, not activated, macrophages suggesting that it plays a role in activation mechanisms of macrophages.

Sugar uptake was measured with 3H-galactose and 14C-glucose. Galactose transport system was not modified by inhibitors of known translocases and did not present a saturation kinetic with high concentration of galactose. Glucose incorporation was inhibited by lasalocid (cation symport inhibitor) and increased by KCl. The kinetic parameters KM and Vmax were respectively 9.16 mM and 26.56 nmol/min/mg cell protein. On the basis of this study, galactose crossed through the membrane by diffusion, and glucose was incorporated by a cation symport which is regulated by K+ ions.

A liquid chromatographic (LC) method is described for quantitative determination of putrefaction amines: putrescine, cadaverine, histamine, spermidine, and spermine. These amines are extracted from fish by grinding with perchloric acid at -20 degrees C. The amines are reacted with dansyl chloride at alkaline pH, dried under a stream of nitrogen, placed in an automatic injector at -20 degrees C, and separated in a Kromasil C18 reversed-phase column at 25 degrees C. A new gradient elutes the amines in 22 min and regenerates the column in 30 min. Regression lines are obtained with high coefficients of correlation. This method is faster and more reproducible than other methods and shows that the quality index is a reliable, albeit species-specific, criterion of fish decomposition.

During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines. These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies. Their structures have been established by 400 MHz 1H-NMR spectroscopy. These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins. Their structures are discussed in the context of the known catabolic pathways of N-glycans.

Nitration of tyrosine residues was performed on Bacillus circulans E 192 cyclomaltodextrin glucanotransferase (CGTase) using tetranitromethane (TNM). A maximum of 15 out of 28 tyrosine residues is modified with 8 mM TNM, entailing a concomitant loss of enzymic activity and tryptophan fluorescence. Spectroscopic studies suggest that these two phenomena are related to an impairment of the enzyme conformation as a consequence of the tyrosine nitration. The presence of 5 mM acarbose during the CGTase nitration results in the protection of one tyrosine residue and the rate of inactivation is reduced 9.4-fold. These results support a contribution of a tyrosine residue in the CGTase catalytic site. The nitration of CGTase also entails a decrease in the enzyme's affinity for a beta-cyclodextrin (beta-CD) co-polymer. Kinetic and analytical investigations on isolated modified enzymes support the concept that this phenomenon is unrelated to the modification of tyrosine residues, but rather concerns a side reaction of the reagent occurring at the raw-starch-binding site of the CGTase.

Oligosaccharides formed by a transgalactosylation reaction during lactose hydrolysis with Bifidobacterium bifidum were separated into eight fractions by gel-permeation chromatography and their structures studies determined by trimethylsilylation analysis, methylation analysis, f.a.b.-m.s., g.l.c.-m.s. and enzymic hydrolysis as beta-D-Galp-(1----3)-D-Glc, beta-D-Galp-(1----6)-D-Glc, beta-D-Galp-(1----6)-D-Gal, beta-D-Galp-(1----3)-beta-D-Galp-(1----4)-D-Glc, beta-D-Galp-(1----6)[beta-D-Galp-(1----4)]-D-Glc, beta-D-Galp-(1----2)[beta-D-Galp-(1----6)]-D-Glc, beta-D-Galp-(1----3)-beta-D-Galp-(1----3)-beta-D-Galp-(1----4)-D-Glc, beta-D-Galp-(1----3)-beta-D-Galp-(1----3)-beta-D-Galp-(1----3)-beta-D-Ga lp- (1----4)-D-Glc, beta-D-Galp-(1----3)-beta-D-Galp-(1----3)-beta-DGalp-(1----3)-beta -D-Galp-(1----3)-beta-D-Galp-(1----4)-D-Glc, and beta-D-Galp-(1----3)-beta-D-Galp-(1----3)-beta-D-Galp-(1----3)-beta-D-Ga lp-(1----3)-beta-D-G-alp-(1----3) beta-D-Galp-(1----4)-D-Glc.

An abnormal carbohydrate pattern was found in urine of a patient with early myoclonic epileptic encephalopathy. Three major oligosaccharides have been isolated from the urine; structural studies including sugar analyses, methylation procedure and enzymatic hydrolysis allow us to propose the following structures: beta-Gal-(1 leads to 3)-Gal beta-Gal-(1 leads to 3)-beta-Gal-(1 leads to 3)-Glc beta-Gal-(1 leads to 3)-beta-Gal-(1 leads to 3)-Gal Such oligosaccharide structures have not previously been described in any biological fluid. The origin of these compounds, and the possibility of a specific metabolic defect are discussed.

Mannose-rich oligosaccharides have been isolated from urines of 5 patients with mannosidosis. Their compositon and structure were determined. Three of them have been previously described by Norden et al: alpha p-Manp-(1 leads to 3) beta-d-Manp-(1 leads to 4) d-GlcNAcp; alpha-p-Manp-(1 leads to 2), alpha-d-Manp-(1 leads to 3) beta-d-Manp-(1 leads to 4) d-GlcNAc and alpha-d-Manp-(1 leads to 2) alpha-d-Manp-(1 leads to 2) alpha-d-Manp-(1 leads to 3) beta-d-Manp-(1 leads to 4) d-GlcNAcp, but the four others are new entities: alpha-d-Manp-(1 leads to 3) (alpha-d-Manp-(1 leads to 2) alpha-d-Manp-(1 leads to 2) alpha-d-Manp-(1 leads to 6) beta-d-Manp-(1 leads to 4) GlcNAcp; alpha-d-Manp-(1 leads to 2) alpha-d-Manp-(1 leads to 3) (alpha-d-Manp-(1 leads to 2) alpha-d-Manp-(1 leads to 6) beta-d-Manp-(1 leads to 4) GlcNAcp; alpha-d-Manp-(1 leads to 2), alpha-d-Man-(1 leads to 3) (alpha-d-Manp-(1 leads to 6) beta-d-Manp-(1 leads to 4) GlcNAp and alpha-d-Manp-(1 leads to 2) alpha-d-Manp-(1 leads to 3) (alpha-d-Manp-(1 leads to 6) beta-d-Manp-(1 leads to 4) GlcNAcp. These structures are related to the glycans of "oligomannosidic type" present in numerous glycoproteins. All possess a N-acetylglucosamine residue in terminal reducing position and reinforce the hypothesis of Kobata et al. and Montreuil et al. that catabolism of glycans N-glucosidically linked to the protein moiety begins by the aciton of a beta-endo-N-acetylglucosaminidase.

The polypeptide chain of human lactotransferrin possesses two glycoslyation sites to which glycans are linked through an N-(beta-aspartyl)-N-acetylglucosaminylamine bond and which are structurally heterogenous. After chymotryptic or pronase digestions, glycopeptides with five different glycan structures could be isolated. For three of them, the structure has been determined by the application of methanolysis, methylation analysis, hydrazinolysis/nitrous deamination, enzymatic cleavage and 1H-NMR spectroscopy at 360 MHz: Glycopeptides A and B: NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)[NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-6)]Man(beta 1-4)GlcNAc(beta-1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-)Asn; Glycopeptide C: NeuAc(alpha 2-6)(Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)(Gal(beta 1-4)[Fuc(alpha 1-3)]GlcNAc(beta 1-2)Man(alpha 1-6))Man(beta 1-4)GlcNAc(beta 1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-)Asn. Glycopeptide D: NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)[Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-6)]Man(beta 1-4)Glc-NAc(beta 1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-)Asn. Two other glycopeptides were obtained in very low amount and possess more complex structures.

Induced galactosuria is characterized by the excretion in urine of large amounts of new oligosaccharides, the structure of which are in connection with blood-group phenotypes ABH, Lewis and Secretor: O group : O-alpha-L fucopyranosyl-(1 leads to 2)-D galactopyranose et O-alpha-L fucopyranosyl-(1 leads to 2)-O-beta-D galactopyranosyl-(1 leads to 3)-[O-alpha-L fucopyranosyl-(1 leads to 4)]-O-beta-D 2-deoxy-2 acetamido-glucopyranosyl-(1 leads to 4)-[O-alpha-L fucopyranosyl-(1 leads to 6)]-D-galactopyranose. A group: O-alpha-D-2-deoxy-2 acetamido-galactopyranosyl-(1 leads to 3)-[O-alpha-L fucopyranosyl-(1 leads to 2)]-D galactopyranose et O-alpha-D-2-deoxy-2 acetamido-galactopyranosyl-(1 leads to 3)-[O-alpha-L fucopyranosyl-(1 leads to 2)]-O-beta-D galactopyranosyl-(1 leads to 3)-[O-alpha-L fucopyranosyl-(1 leads to 4)]-O-beta-D-2-deoxy-2 acetamido-glucopyranosyl-(1 leads to)-[O-alpha-L fucopyranosyl-(1 leads to 6)]-D galactopyranose. B group : O-alpha-D galactopyranosyl-(1 leads to 3)-[O-alpha-L fucopyranosyl-(1 leads to 2)]-D galactopyranose et O-alpha-D galactopyranosyl-(1 leads to 3)-[O-alpha-L fucopyranosyl-(1 leads to 2)]-O-beta-D galactopyranosyl-(1 leads to 3)-[O-alpha-L fucopyranosyl-(1 leads to 4)]-O-beta-D-2-deoxy-2 acetamido-glucopyranosyl-(1 leads to 4)-[O-alpha-L fucopyranosyl-(1 leads to 6)]-D-galactopyranose.