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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and partial characterization of a lactotransferrin receptor from mouse intestinal brush-border (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 535-541 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00454a030
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactotransferrin (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 9243-9251 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00153a018
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  • 3
    Electronic Resource
    Electronic Resource
    Oligosaccharide structural specificity of the soluble agglutinin released from guinea pig colonic epithelial cells (1983)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 20 (1983), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Guinea pig colonic epithelial cells release a soluble lectin capable of agglutinating numerous strains of Shigella and Escherichia coli as well as other bacteria. Using pure oligosaccharides and glycopeptides with well-defined structures to inhibit the agglutination of Shigella flexneri 1b by the soluble intestinal lectin, we have been able to demonstrate that the latter recognises different structural types. Inhibition by human milk glucoprotein glycopeptides with biantennary glycans of the N-acetyllactosamine type was dependent on the simultaneous presence of unsubstituted terminal non-reducing galactose residues and of a fucose residue α-1,6-linked to the asparagine-conjugated N-acetylglucosamine residue. Unsubstituted terminal non-reducing galactose was also determinant for inhibition by human milk oligosaccharides. Finally oligosaccharides possessing the Man (α1–2) Man structure inhibited more effectively than those with a Man(α1–3)Man sequence. The fact that these different structural motifs were all inhibitory raises the problem of the possible existence of a multispecific lectin or of several different lectins in the guinea pig colonic mucosa mediating bacterial adherence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1983.tb00124.x
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation of 4-acetamido-2-amino-2,4,6-trideoxy-glucose (N-acetylbacillosamine) from a polysaccharide of Bacillus amyloliquefaciens (1983)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 20 (1983), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1983.tb00087.x
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  • 5
    Electronic Resource
    Electronic Resource
    Receptor-Mediated Transcytosis of Cyclophilin B Through the Blood—Brain Barrier (1999)
    Oxford UK : Blackwell Science Ltd
    Journal of neurochemistry 73 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Cyclophilin B (CyPB) is a cyclosporin A (CsA)-binding protein mainly located in intracellular vesicles and secreted in biological fluids. In previous works, we demonstrated that CyPB interacts with T lymphocytes and enhances in vitro cellular incorporation and activity of CsA. In addition to its immunosuppressive activity, CsA is able to promote regeneration of damaged peripheral nerves. However, the crossing of the drug from plasma to neural tissue is restricted by the relative impermeability of the blood—brain barrier. To know whether CyPB might also participate in the delivery of CsA into the brain, we have analyzed the interactions of CyPB with brain capillary endothelial cells. First, we demonstrated that CyPB binds to two types of binding sites present at the surface of capillary endothelial cells from various species of tissues. The first type of binding sites (KD = 300 nM; number of sites = 3 × 106) is related to interactions with negatively charged compounds such as proteoglycans. The second type of binding sites, ∼50,000 per cell, exhibits a higher affinity for CyPB (KD = 15 nM) and is involved in an endocytosis process, indicating it might correspond to a functional receptor. Finally, the use of an in vitro model of blood—brain barrier allowed us to demonstrate that CyPB is transcytosed by a receptor-mediated pathway (flux = 16.5 fmol/cm2/h). In these conditions, CyPB did not significantly modify the passage of CsA, indicating that it is unlikely to provide a pathway for CsA brain delivery.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0730260.x
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of sheep hemopexin glycovariants (1995)
    Springer
    Glycoconjugate journal 12 (1995), S. 645-650 
    Details
    ISSN: 1573-4986
    Keywords: sheep hemopexin ; glycoform ; 1H-NMR spectroscopy ; glycan structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The hemopexin phenotype HpxB1 isolated from sheep serum, yields three major bands when subjected to starch gel and/or polyacrylamide gel electrophoresis which are here designated as subcomponents HpxB1-I, HpxB1-II and HpxB1-III. Electrospray mass spectrometric analysis of samples of the isolated subcomponents prepared by ion exchange chromatography showed that each was composed of three glycoproteins and that the major difference between the subcomponents was due to their constituent glycoproteins possessing different numbers of sialic acid residues. Combined analysis of the ESI-MS data and of the overall carbohydrate compositional data obtained by colorimetric procedures, leads to the composition of the glycan of each glycoprotein, and a combined methylation and 400 MHz H-NMR analysis of the alkaline cleaved glycans identified them as being of only the biantennaryN-acetyllactosamine type. Taking into account the molecular mass, the carbohydrate content and structure it may be concluded that each of the constituent glycoproteins contain fiveN-glycosidically linked glycans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731260
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  • 7
    Electronic Resource
    Electronic Resource
    Structure of the O-glycopeptides isolated from bovine milk component PP3 (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 371-378 
    Details
    ISSN: 1573-4986
    Keywords: bovine milk ; lactophorin ; proteose peptone ; component PP3 ; O-glycan ; ConA, concanavalin A ; GlyCAM, glycosylation-dependent cell adhesion molecule ; HPAE, high-pH anion-exchange, MFGM, milk fat globule membrane ; PP, proteose peptone.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The heat-stable acid-soluble phosphoglycoprotein component PP3 was isolated from the bovine milk proteose peptone fraction by concanavalin A affinity chromatography. Glycopeptides from the ConA-bound fraction corresponding to the component PP3 were obtained by Pronase digestion and were separated by gel filtration into high and low-molecular-mass glycopeptides. In a previous work, we have investigated the structure of the N-glycans from the high-molecular-mass glycopeptides [Girardet et al. (1995) Eur J Biochem 234: 939–46]. Here, we describe the structure of the O-glycans from the low-molecular-mass glycopeptides. By combining methylation analysis, mass spectrometry, 400 MHz 1H-NMR spectroscopy and peptide sequence analysis, we show that the low-molecular-mass fraction contains several neutral glycopeptides. A mixture of the following three glycan structures linked to the Thr86 has been identified: GalNacα1-O-Thr, Gal(β1-3)GalNAcα1-O-Thr and Gal(β1-4)GlcNAc(β1-6)[Galβ1-3)]GalNAcα1-O-Thr. © 1998 Rapid Science Ltd
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006973802139
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  • 8
    Electronic Resource
    Electronic Resource
    Specificity towards oligomannoside and hybrid type glycans of the endo-β-N-acetylglucosaminidase B from the basidiomy ceteSporotrichum dimorphosporum (1989)
    Springer
    Glycoconjugate journal 6 (1989), S. 333-348 
    Details
    ISSN: 1573-4986
    Keywords: glycosidases ; endoglycosidase ; endo-β-N-acetylglucosaminidase ; glycoproteins ; glycans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We have previously shown that an endo-β-N-acetylglucosaminidase (EC 3.2.1.96) named “Endo B”, isolated from culture filtrates of the basidiomyceteSporotrichum dimorphosporum cleaves asialo-, and to some extent, monosialylated bi-antennary glycans of theN-acetyllactosamine type linked to the asparagine residue of peptide or protein moieties [Bouquelet S, Strecker G, Montreuil J, Spik G (1980) Biochimie 62:43–49]. In the present paper, the substrate specificity of the enzyme towards oligomannoside and hybrid type glycans has been analyzed. The results obtained indicate that ovalbumin glycopeptides containing four to seven mannose residues and bovine lactotransferrin glycopeptides containing four to nine mannose residues were completely hydrolyzed by the enzyme. The degree of cleavage was variable among hybrid type structures, since glycopeptides containing the following glycans: (Gal)1(GlcNAc)3(Man)5(GlcNAc)2; (GlcNAc)3(Man)5(GlcNAc)2; (GlcNAc)3(Man)4(GlcNAc)2 were not hydrolyzed by the enzyme while the percentage of hydrolysis of a glycopeptide containing (GlcNAc)2(Man)5(GlcNAc)2 glycan reached 90%. The bovine lactotransferrin was partially deglycosylated (40%) in the absence of non-ionic detergent while native ovalbumin glycoprotein was not hydrolyzed by the enzyme. The oligomannoside-and theN-acetyllactosamine-type degrading activities present in the culture filtrates were not separated at any step of the purification procedure. Both activities were eluted as a single component with an apparent molecular mass of 89 kDa suggesting that they are located on the same enzyme molecule. Endo B represents a powerful tool for removing oligomannoside-andN-acetyllactosamine-type glycans fromN-glycopeptides andN-glycoproteins. Moreover, advantages in the use of Endo B in a soluble form as well as in an immobilized form result in its high activity and in its stability to heat denaturation and storage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01047852
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  • 9
    Electronic Resource
    Electronic Resource
    Determination of glycan structures and molecular masses of the glycovariants of serum transferrin from a patient with carbohydrate deficient syndrome type II (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 265-273 
    Details
    ISSN: 1573-4986
    Keywords: carbohydrate deficiency glycoprotein syndrome ; electrospray ; glycan structure ; glycoforms ; transferrin ; CDG, carbohydrate deficient glycoprotein ; Tf, transferrin ; FPLC, fast protein liquid chromatography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Serum transferrin from a child with carbohydrate deficient syndrome type II was isolated by immunoaffinity chromatography and separated into minor and major fractions by fast protein liquid chromatography. The structure of the glycans released from the major fraction by hydrazinolysis was established by application of methanolysis and 1H-NMR spectroscopy. The results led to the identification of an N-acetyllactosamininic type monosialylated, monoantennary Man(α1-3) linked glycan. By electrospray-mass spectrometry analysis, the whole serum transferrin was separated into at least seven species (I to VII) with molecular masses ranging from 77 958 to 79 130 Da. On the basis of a polypeptide chain molecular mass of 75 143 Da, it was calculated that the major transferrin species III (78 247 Da) contains two monosialylated monoantennary glycans. The molecular mass of transferrin species V and VI (78 678 and 78 971 Da) suggests that one of their two glycans contains an additional N-acetyllactosamine and a sialylated N-acetyllactosamine units, respectively. Transferrin species I and V were found to correspond to the desialylated forms of species III and VI. The abnormal glycan structures can be explained by a defect in the N-acetylglucosaminyltransferase II activity [Charuk et al. (1995) Eur J Biochem 230: 797-805].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006997012617
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular modeling of a disialylated monofucosylated biantennary glycan of theN-acetyllactosamine type (1991)
    Springer
    Glycoconjugate journal 8 (1991), S. 390-399 
    Details
    ISSN: 1573-4986
    Keywords: molecular modeling ; glycan ; glycoprotein ; three dimensional structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The conformations of a disialylated monofucosylated biantennary glycan of theN-acetyllactosamine type were analysed using the Tripos 5.3 force field from the Sybyl software currently used for molecular modelling. The conformation of each glycosidic linkage was calculated when included in oligosaccharide structures of up to 5 units and the influence of the glycosidic environment on the overall structure was measured. The study clearly shows that the conformation of a branched glycan cannot result from the simple addition of the different low energy conformers of each of the glycosidic linkages constituting the glycan structure. The asymmetrical conformation of the two antennae was demonstrated. The lowest energy conformations of the overall glycan structure were built and classified into 5 main models: the Y, T, bird and broken wing conformations already described and a new one called the ‘back folded wing conformation’.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731291
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