InChI=1S/C25H42N2O19/c1- 7(30)26-13-9(32)3-25(24(40)41,46-21(13)15(34)10(33)4-28)42-6-12-16(35)18(37)19(38)23(44-12)45-20-11(5-29)43-22(39)14(17(20)36)27-8(2)31/h9-23,28-29,32-39H,3-6H2,1-2H3,(H,26,30)(H,27,31)(H,40,41)/t9-,10+,11+,12+,13+,14+,15+,16-,17+,18-,19+,20+,21+,22+,23-,25+/m0/s1 |
| RPSBVJXBTXEJJG-LURNZOHQSA-N |
| [H][C@]1(O[C@@](C[C@H](O)[C@H]1NC(C)=O)(OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](NC(C)=O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O)C(O)=O)[C@H](O)[C@H](O)CO |
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epitope
The biological role played by a material entity when bound by a receptor of the adaptive immune system. Specific site on an antigen to which an antibody binds.
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View more via ChEBI Ontology
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Outgoing
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α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine
(CHEBI:17725)
has role
epitope
(CHEBI:53000)
α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine
(CHEBI:17725)
is a
amino trisaccharide
(CHEBI:59266)
α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine
(CHEBI:17725)
is a
glucosamine oligosaccharide
(CHEBI:22485)
α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine
(CHEBI:17725)
is conjugate acid of
α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine(1−)
(CHEBI:60040)
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Incoming
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α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine(1−)
(CHEBI:60040)
is conjugate base of
α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine
(CHEBI:17725)
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5-acetamido-3,5-dideoxy-D-glycero-α-D-galacto-non-2-ulopyranonosyl-(2→6)-β-D-galactopyranosyl-(1→4)-2-acetamido-2-deoxy-β-D-glucopyranose
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(2R,4S,5R,6R)-5-acetamido-2-{[(2R,3R,4S,5R,6S)-6-{[(2R,3S,4R,5R,6R)-5-acetamido-4,6-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy}-3,4,5-trihydroxyoxan-2-yl]methoxy}-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid
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HMDB
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(N-acetylneuraminosyl(alpha2-6)lactosamine)
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HMDB
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6'-Sialyllactosamine
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HMDB
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6-Sialyllactosamine
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ChemIDplus
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alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
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ChEBI
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alpha-N-Acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
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KEGG COMPOUND
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alpha-N-Acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
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HMDB
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alpha-N-Acetylneuraminyl-2,6-beta-delta-galactosyl-1,4-N-acetyl-beta-delta-glucosamine
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HMDB
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α-NeuNAc-(2→6)-β-D-Gal-(1→4)-β-D-GlcNAc
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ChEBI
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α-NeupNAc-(2→6)-β-D-Galp-(1→4)-β-D-GlcpNAc
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ChEBI
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N-Acetylneuraminosyl(alpha2-6)lactosamine
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ChemIDplus
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Neu5Aca2-6Galb1-4GlcNAcb
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ChEBI
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Neuac-lact
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ChemIDplus
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NeuAcalpha2,6Galbeta1,4GlcNAc
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HMDB
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Neuacalpha2,6GalNAcbeta1,4GlcNAc
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ChemIDplus
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Neuacalpha2-6Galbeta1-4GlcNAcbeta
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ChemIDplus
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O-(N-Acetyl-a-neuraminosyl)-(2→6)-O-b-D-galactopyranosyl-(1→4)-2-(acetylamino)-2-deoxy-b-D-Glucopyranose
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HMDB
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O-(N-Acetyl-alpha-neuraminosyl)-(26)-O-beta-D-galactopyranosyl-(1→-4)-2-(acetylamino)-2-deoxy-beta-D-Glucopyranose
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HMDB
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O-(N-Acetyl-alpha-neuraminosyl)-(2→6)-O-beta-delta-galactopyranosyl-(1→-4)-2-(acetylamino)-2-deoxy-beta-delta-Glucopyranose
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HMDB
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O-5-(acetylamino)-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranonosyl-(2→6)-O-β-D-galactopyranosyl-(1→4)-2-(acetylamino)-2-deoxy-β-D-glucopyranose
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ChEBI
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WURCS=2.0/3,3,2/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O]/1-2-3/a4-b1_b6-c2
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GlyTouCan
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5721087
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Beilstein Registry Number
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Beilstein
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64364-50-7
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CAS Registry Number
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ChemIDplus
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Jandus P, Boligan KF, Smith DF, de Graauw E, Grimbacher B, Jandus C, Abdelhafez MM, Despont A, Bovin N, Simon D, Rieben R, Simon HU, Cummings RD, von Gunten S (2019)
The architecture of the IgG anti-carbohydrate repertoire in primary antibody deficiencies.
Blood 134, 1941-1950 [PubMed:31537530]
[show Abstract]
Immune system failure in primary antibody deficiencies (PADs) has been linked to recurrent infections, autoimmunity, and cancer, yet clinical judgment is often based on the reactivity to a restricted panel of antigens. Previously, we demonstrated that the human repertoire of carbohydrate-specific immunoglobulin G (IgG) exhibits modular organization related to glycan epitope structure. The current study compares the glycan-specific IgG repertoires between different PAD entities. Distinct repertoire profiles with extensive qualitative glycan-recognition defects were observed, which are characterized by the common loss of Galα and GalNAc reactivity and disease-specific recognition of microbial antigens, self-antigens, and tumor-associated carbohydrate antigens. Antibody repertoire analysis may provide a useful tool to elucidate the degree and the clinical implications of immune system failure in individual patients. | Schneider C, Smith DF, Cummings RD, Boligan KF, Hamilton RG, Bochner BS, Miescher S, Simon HU, Pashov A, Vassilev T, von Gunten S (2015)
The human IgG anti-carbohydrate repertoire exhibits a universal architecture and contains specificity for microbial attachment sites.
Science translational medicine 7, 269ra1 [PubMed:25568069]
[show Abstract]
Despite the paradigm that carbohydrates are T cell-independent antigens, isotype-switched glycan-specific immunoglobulin G (IgG) antibodies and polysaccharide-specific T cells are found in humans. We used a systems-level approach combined with glycan array technology to decipher the repertoire of carbohydrate-specific IgG antibodies in intravenous and subcutaneous immunoglobulin preparations. A strikingly universal architecture of this repertoire with modular organization among different donor populations revealed an association between immunogenicity or tolerance and particular structural features of glycans. Antibodies were identified with specificity not only for microbial antigens but also for a broad spectrum of host glycans that serve as attachment sites for viral and bacterial pathogens and/or exotoxins. Tumor-associated carbohydrate antigens were differentially detected by IgG antibodies, whereas non-IgG2 reactivity was predominantly absent. Our study highlights the power of systems biology approaches to analyze immune responses and reveals potential glycan antigen determinants that are relevant to vaccine design, diagnostic assays, and antibody-based therapies. | von Gunten S, Smith DF, Cummings RD, Riedel S, Miescher S, Schaub A, Hamilton RG, Bochner BS (2009)
Intravenous immunoglobulin contains a broad repertoire of anticarbohydrate antibodies that is not restricted to the IgG2 subclass.
The Journal of allergy and clinical immunology 123, 1268-76.e15 [PubMed:19443021]
[show Abstract]
BackgroundSpecificities for carbohydrate IgG antibodies, thought to be predominantly of the IgG2 subclass, have never been broadly examined in healthy human subjects.ObjectiveTo examine commercial intravenous immunoglobulin (IVIG) preparations for their ability to recognize a wide range of glycans and to determine the contribution of IgG2 to the binding pattern observed.MethodsWe used a glycan microarray to evaluate IVIG preparations and a control mix of similar proportions of human myeloma IgG1 and IgG2 for binding to 377 glycans, courtesy of the Consortium for Functional Glycomics Core H. Glycans recognized were categorized using public databases for their likely cellular sources. IgG2 was depleted from IVIG by using immunoaffinity chromatography, and depletion was confirmed by using nephelometry and surface plasmon resonance.ResultsNearly half of the glycans bound IgG. Some of the glycans with the greatest antibody binding can be found in structures of human pathogenic bacteria (eg, Streptococcus pneumoniae, Mycobacterium tuberculosis, Vibrio cholera) and nonpathogenic bacteria, including LPS and lipoteichoic acid, capsular polysaccharides, and exopolysaccharides. Surprisingly, depletion of IgG2 had only a modest effect on anticarbohydrate recognition patterns compared with the starting IVIG preparation. Little to no binding activity was detected to human endogenous glycans, including tumor-associated antigens.ConclusionsThis novel, comprehensive analysis provides evidence that IVIG contains a much wider range than previously appreciated of anticarbohydrate IgG antibodies, including those recognizing both pathogenic and non-pathogen-associated prokaryotic glycans. | Mochalova L, Gambaryan A, Romanova J, Tuzikov A, Chinarev A, Katinger D, Katinger H, Egorov A, Bovin N (2003)
Receptor-binding properties of modern human influenza viruses primarily isolated in Vero and MDCK cells and chicken embryonated eggs.
Virology 313, 473-480 [PubMed:12954214]
[show Abstract]
To study the receptor specificity of modern human influenza H1N1 and H3N2 viruses, the analogs of natural receptors, namely sialyloligosaccharides conjugated with high molecular weight (about 1500 kDa) polyacrylamide as biotinylated and label-free probes, have been used. Viruses isolated from clinical specimens were grown in African green monkey kidney (Vero) or Madin-Darby canine kidney (MDCK) cells and chicken embryonated eggs. All Vero-derived viruses had hemagglutinin (HA) sequences indistinguishable from original viruses present in clinical samples, but HAs of three of seven tested MDCK-derived isolates had one or two amino acid substitutions. Despite these host-dependent mutations and differences in the structure of HA molecules of individual strains, all studied Vero- and MDCK-isolated viruses bound to Neu5Ac alpha2-6Galbeta1-4GlcNAc (6'SLN) essentially stronger than to Neu5Acalpha2-6Galbeta1-4Glc (6'SL). Such receptor-binding specificity has been typical for earlier isolated H1N1 human influenza viruses, but there is a new property of H3N2 viruses that has been circulating in the human population during recent years. Propagation of human viruses in chicken embryonated eggs resulted in a selection of variants with amino acid substitutions near the HA receptor-binding site, namely Gln226Arg or Asp225Gly for H1N1 viruses and Leu194Ile and Arg220Ser for H3N2 viruses. These HA mutations disturb the observed strict 6'SLN specificity of recent human influenza viruses. | Toma V, Zuber C, Winter HC, Goldstein IJ, Roth J (2001)
Application of a lectin from the mushroom Polysporus squamosus for the histochemical detection of the NeuAcalpha2,6Galbeta1,4Glc/GlcNAc sequence of N-linked oligosaccharides: a comparison with the Sambucus nigra lectin.
Histochemistry and cell biology 116, 183-193 [PubMed:11685546]
[show Abstract]
The lectin from the mushroom Polysporus squamosus (PSL) has an extended carbohydrate combining site, which exhibits a high specificity and affinity toward the NeuAc5alpha2,6Galbeta1,4Glc/GlcNAc trisaccharide sequence of asparagine-linked oligosaccharides. Therefore, PSL should be a superior reagent to the lectin from Sambucus nigra (SNA), which does not discriminate between alpha2,6-linked NeuAc5 present either in asparagine- or serine/threonine-linked oligosaccharides. We have prepared a digoxigenin-conjugated PSL and applied it for histochemistry and blotting. We observed a more restricted staining pattern by PSL as compared to SNA in paraffin sections from different rat organs. Pretreatment of sections with N-glycanase F abolished PSL staining indicating that it interacts only with asparagine-linked oligosaccharides. Furthermore, PSL staining was neuraminidase sensitive. In contrast, SNA staining was only partially sensitive to N-glycanase F pretreatment demonstrating that it was in part due to alpha2,6-linked NeuAc5 present in serine/threonine-linked oligosaccharides. The most striking observation in this regard was that PSL, in contrast to SNA, did not stain the mucus of sheep submandibular gland, which is extremely rich in serine/threonine-linked Neu5Acalpha2,6N-acetylgalactosamine. Furthermore, in some tissues neuraminidase pretreatment resulted in increased intensity of SNA staining probably due to binding to exposed terminal N-acetylgalactosamine residues. Collectively, these results indicate that PSL is a useful tool for the histochemical detection of alpha2,6-linked NeuAc5 in asparagine-linked oligosaccharides. | Shen Z, Warren CD, Newburg DS (2000)
High-performance capillary electrophoresis of sialylated oligosaccharides of human milk.
Analytical biochemistry 279, 37-45 [PubMed:10683228]
[show Abstract]
Oligosaccharides in human milk inhibit enteric pathogens in vitro and in vivo. Neutral milk oligosaccharides vary among individuals and over the course of lactation. To study such variation in the acidic milk oligosaccharides, a sensitive, convenient, quantitative method is needed. High-performance capillary electrophoresis of underivatized acidic oligosaccharides with detection by UV absorbance at 205 nm proved to be sensitive to the femtomole level. Eleven standard oligosaccharides ranging from tri- to nonasaccharide (3'-sialyllactose, 6'-sialyllactose, 3'-sialyllactosamine, 6'-sialyllactosamine, disialyltetraose, 3'-sialyl-3-fucosyllactose, sialyllacto-N-tetraose-a, sialyllacto-N-tetraose-b, sialyllacto-N-neotetraose-c, disialyllacto-N-tetraose, and disialomonofucosyllacto-N-neohexaose) were resolved; baseline resolutions of 3'-sialyllactose, 6'-sialyllactose, and other structural isomers were achieved. Peak areas were linear from 30 to 2000 pg and were reproducible with a coefficient of variation between 4 and 9%. There was no evidence of quantitative interference of one oligosaccharide with another. In studies using pooled human milk, addition of increasing amounts of authentic standard oligosaccharides produced the expected positive increments in detected values, indicating quantitative recovery without interference by other milk components. The identities of the major sialylated acidic oligosaccharides of pooled human milk agreed with the results of previous studies employing other analytical methods. Comparison of oligosaccharide profiles of milk samples from different donors revealed extensive variation, especially in the structural isomers of sialyllacto-N-tetraose. This sensitive, highly reproducible method requires only simple sample workup and is useful in defining variations in human milk acidic oligosaccharides and investigating their possible relationship with diseases of infants. | Kunz C, Rudloff S, Baier W, Klein N, Strobel S (2000)
Oligosaccharides in human milk: structural, functional, and metabolic aspects.
Annual review of nutrition 20, 699-722 [PubMed:10940350]
[show Abstract]
Research on human milk oligosaccharides (HMOs) has received much attention in recent years. However, it started about a century ago with the observation that oligosaccharides might be growth factors for a so-called bifidus flora in breast-fed infants and extends to the recent finding of cell adhesion molecules in human milk. The latter are involved in inflammatory events recognizing carbohydrate sequences that also can be found in human milk. The similarities between epithelial cell surface carbohydrates and oligosaccharides in human milk strengthen the idea that specific interactions of those oligosaccharides with pathogenic microorganisms do occur preventing the attachment of microbes to epithelial cells. HMOs may act as soluble receptors for different pathogens, thus increasing the resistance of breast-fed infants. However, we need to know more about the metabolism of oligosaccharides in the gastrointestinal tract. How far are oligosaccharides degraded by intestinal enzymes and does oligosaccharide processing (e.g. degradation, synthesis, and elongation of core structures) occur in intestinal epithelial cells? Further research on HMOs is certainly needed to increase our knowledge of infant nutrition as it is affected by complex oligosaccharides. | Dall'Olio F (2000)
The sialyl-alpha2,6-lactosaminyl-structure: biosynthesis and functional role.
Glycoconjugate journal 17, 669-676 [PubMed:11425186]
[show Abstract]
Sialylation represents one of the most frequently occurring terminations of the oligosaccharide chains of glycoproteins and glycolipids. Sialic acid is commonly found alpha2,3- or alpha2,6-linked to galactose (Gal), alpha2,6-linked to N-acetylgalactosamine (GalNAc) or alpha2,8-linked to another sialic acid. The biosynthesis of the various linkages is mediated by the different members of the sialyltransferase family. The addition of sialic acid in alpha2,6-linkage to the galactose residue of lactosamine (type 2 chains) is catalyzed by beta-galactoside alpha2,6-sialyltransferase (ST6Gal.I). Although expressed by a single gene, this enzyme shows a complex pattern of regulation which allows its tissue- and stage-specific modulation. The cognate oligosaccharide structure, NeuAcalpha2,6Galbeta1,4GlcNAc, is widely distributed among tissues and is involved in biological processes such as the regulation of the immune response and the progression of colon cancer. This review summarizes the current knowledge on the biochemistry of ST6Gal.I and on the functional role of the sialyl-alpha2,6-lactosaminyl structure. | Huynh QK, Shailubhai K, Boddupalli H, Yu HH, Broschat KO, Jacob GS (1999)
Isolation and characterization from porcine serum of a soluble sulfotransferase responsible for 6-O-sulfation of the galactose residue in 2'-fucosyllactose: implications in the synthesis of the ligand for L-selectin.
Glycoconjugate journal 16, 357-363 [PubMed:10619708]
[show Abstract]
A soluble sulfotransferase from porcine serum which catalyzes the transfer of sulfate from adenosine 3'-phosphate 5'-phosphosulphate (PAPS) to 2'-fucosyllactose (2'-FL) was purified 36,333-fold using a combination of conventional and affinity chromatographic steps. The purified enzyme preparation after non-denaturing discontinuous-PAGE exhibited a molecular mass of about 80 kDa by reducing SDS-PAGE. However, when a partially purified enzyme preparation was subjected to gel filtration on Sephacryl S-300, the enzyme activity eluted in the void volume, which indicated that the native enzyme existed as an oligomer. The purified enzyme showed Km values of 9.15 microM for PAPS and 15.38 mM for 2'-FL at the optimum pH value of 7.4. The substrate specificity of the purified enzyme was evaluated with various sugars that are structurally similar to sialyl LewisX (sLeX). Results indicated that 3'-sialyllactose and lactose were efficient acceptors of sulfation, whereas 6'-sialyllactose and 6'-sialyllactosamine were poor substrates for this sulfotransferase. Further, the reaction product analysis revealed that the sulfate substitution, when using 2'-FL as the substrate, was at the C-6 position of the galactose residue. Coincidentally, a similar enzyme activity was also found in porcine lymphoid tissues such as, lymph nodes (peripheral and mesenteric) and spleen. Collectively, these findings suggest that this enzyme might be involved in the synthesis of the ligand for L-selectin. |
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