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  • 1
    Electronic Resource
    Electronic Resource
    Three novel oligosaccharides with the sialyl-Lea structure in human milk: isolation by immunoaffinity chromatography (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 8891-8897 
    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/bi00448a031
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  • 2
    Electronic Resource
    Electronic Resource
    Novel oligosaccharides with the sialyl-Lea structure in human milk (1991)
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 2869-2876 
    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/bi00225a020
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  • 3
    Electronic Resource
    Electronic Resource
    An automated prediction of MHC class I-binding peptides based on positional scanning with peptide libraries (2000)
    Springer
    Immunogenetics 51 (2000), S. 816-828 
    Details
    ISSN: 1432-1211
    Keywords: MHC class I Peptide Library Prediction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Specificities of three mouse major histocompatibility complex (MHC) class I molecules, Kb, Db, and Ld, were analyzed by positional scanning using combinatorial peptide libraries. The result of the analysis was used to create a scoring program to predict MHC-binding peptides in proteins. The capacity of the scoring was then challenged with a number of peptides by comparing the prediction with the experimental binding. The score and the experimental binding exhibited a linear correlation but with substantial deviations of data points. Statistically, for approximately 80% of randomly chosen peptides, MHC-binding capacity could be predicted within one log concentration of peptides for a half-maximal binding. Known cytotoxic T-lymphocyte epitope peptides could be predicted, with a few exceptions. In addition, frequent findings of MHC-binding peptides with incomplete or no anchor amino acid(s) suggested a substantial bias introduced by natural antigen processing in peptide selection by MHC class I molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510000217
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  • 4
    Electronic Resource
    Electronic Resource
    Anhydrous and water-saturated melting experiments of an olivine andesite from Mt Yakushi-Yama, northeastern Shikoku, Japan (1993)
    Oxford, UK : Blackwell Publishing Ltd
    The @island arc 2 (1993), S. 0 
    Details
    ISSN: 1440-1738
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences
    Notes: Abstract Melting experiments have been carried out on an olivine andesite of Mt Yakushi-Yama from the Miocene Setouchi volcanic belt in northeastern Shikoku, Japan. This andesite has been characterized by a low ratio of FeO*/Mg° (= 0.78). Phase relations have been determined within the pressure range of 2.8 to 19.3 kbar at 1000-1300°C under anhydrous and water-saturated conditions. At pressures less than 8.8 kbar, olivine is a liquidus phase. Orthopyroxene appears on the liquidus at 9.3 kbar under the anhydrous conditions. The multiple saturation point rises up to 17.5 kbar for water-saturated experiments. The andesite melt coexists with olivine and orthopyroxene just below the liquidus at 8.8–9.3 kbar and 1230°C for dry conditions, and at 17.5 kbar and 1060°C under water-saturated conditions. These experimental results indicate that the Yakushi-Yama olivine andesite magma could coexist with a harzburgitic mantle at depths between about 30 and 60 km, and at temperatures between 1060 and 1230°C. Experimental data also suggest a possibility that a high magnesian andesite magma would be generated by a direct partial melting of the uppermost harzburgitic mantle under anhydrous conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1738.1993.tb00089.x
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  • 5
    Electronic Resource
    Electronic Resource
    Complement-dependent cytotoxic activity of serum mannan-binding protein towards mammalian cells with surface-exposed high-mannose type glycans (1994)
    Springer
    Glycoconjugate journal 11 (1994), S. 304-308 
    Details
    ISSN: 1573-4986
    Keywords: serum lectin ; complement activation ; cytotoxicity ; 1-deoxymannojirimycin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Serum mannan-binding protein (S-MBP), a lectin specific for mannose andN-acetylglucosamine, activates complement through the classical pathway. With the help of complement, S-MBP lyses red blood cells which have been coated with yeast mannan and kills bacteria which haveN-acetylglucosamine and/orl-glycero-d-manno-heptose on their core oligosaccharide. In this study, we examined whether mammalian cells, on which S-MBP could bound, are killed by a complement-dependent mechanism. When baby hamster kidney (BHK) cells were treated with an α-mannosidase inhibitor, 1-deoxymannojirimycin (dMM), most of the cellular oligosaccharides were transformed from the complex-type to the high mannose-type. S-MBP bound to the dMM-treated BHK cells in the presence of Ca2+, and this binding was eliminated by mannose. When dMM-treated cells, labelled with51Cr, were incubated with complement, radioactivity was released in a dose-dependent manner by S-MBP and complement. This release was not observed with heat-inactivated complement. These observations suggest that S-MBP is able, with the help of complement, to kill not only exogenous microorganisms but also mammalian cells which have high mannose-type oligosaccharides exposed on their surfaces.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731203
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  • 6
    Electronic Resource
    Electronic Resource
    The differences in structural specificity for recognition and binding between asialoglycoprotein receptors of liver and macrophages (1995)
    Springer
    Glycoconjugate journal 12 (1995), S. 268-274 
    Details
    ISSN: 1573-4986
    Keywords: asialoglycoprotein receptor ; rat liver ; rat macrophages ; neoglycoproteins ; synthetic clustered glycosides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The Gal/GalNAc-specific lectin on the surface of rat peritoneal macrophages (macrophage asialoglycoprotein binding protein, M-ASGP-BP), which consists of a single polypeptide chain of 42 kDa, can form a homooligomeric receptor exhibiting high affinity for asialoorosomucoid (ASOR) [Ozaki K., Ii M., Itoh N., Kawasaki T. (1992)J Biol Chem 267: 9229–35]. In this study, the binding affinity of M-ASGP-BP was studied by using a series of synthetic or natural glycosides as inhibitors of125I-ASOR binding to recombinant M-ASGP-BP expressed on COS-1 cells (rM-ASGP-BP), and the results were compared with those of human hepatic lectin (HHL) on Hep G2 cells. Clustering of multiple Gal (or GalNAc) residues increased the binding affinity to M-ASGP-BP as well as to HHL. In contrast to HHL and other mammalian hepatic lectins, rM-ASGP-BP bound Gal residues tighter than GalNAc residues. A galactose-terminated triantennary N-glycoside, having oneN-acetyl-lactosamine unit on the 6 branch and twoN-acetyl-lactosamine units on the 3 branch of the trimannosyl core structure, showed affinity enhancement of ∼105 over a monovalent ligand for HHL, while the same glycopeptide showed enhancement of about 2000-fold for rM-ASGP-BP. These results suggest that spatial arrangements of sugar combining sites and subunit organization of macrophage and hepatic lectins are different.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731329
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  • 7
    Electronic Resource
    Electronic Resource
    A naturally occurring 46-amino acid deletion of cytidine monophospho-N-acetylneuraminic acid hydroxylase leads to a change in the intracellular distribution of the protein (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 353-358 
    Details
    ISSN: 1573-4986
    Keywords: cytidine monophospho-N-acetylneuraminic acid hydroxylase ; N-acetylneuraminic acid ; N-glycolylneuraminic acid ; membrane transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Cytidine monophospho-N-acetylneuraminic acid (CMP-NeuAc) hydroxylase is a key enzyme for the expression ofN-glycolylneuraminic acid. The molecular cloning of this enzyme from mouse liver has been described in our previous report (Kawano T, Koyama S, Takematsu H, Kozutsumi Y, Kawasaki H, Kawashima S, Kawasaki T, Suzuki A (1995)J Biol Chem 270: 16458–63). During the cDNA cloning, a cDNA containing a truncated open reading frame (ORF) was isolated. This clone encodes a protein of 531 amino acids which lacks 46 amino acids in the middle of the normal full-length protein. The percentage of this mRNA containing the truncated ORF out of the total population of CMP-NeuAc hydroxylase mRNA in various mouse tissues was about 10–25%. The truncated protein was expressed in COS-1 cells, but did not show any enzymatic activity. The truncated protein was localized to the region which appeared to be the endoplasmic reticulum, whereas the full-length protein with normal enzymatic activity was detected in the cytosol. These data suggest that this naturally occurring 46-amino acid deletion leads to a change in the intracellular distribution of CMP-NeuAc hydroxylase, and a loss in the activity of this enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731467
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  • 8
    Electronic Resource
    Electronic Resource
    The N-glycan acceptor specificity of a glucuronyltransferase, GlcAT-P, associated with biosynthesis of the HNK-1 epitope (2000)
    Springer
    Glycoconjugate journal 17 (2000), S. 877-885 
    Details
    ISSN: 1573-4986
    Keywords: HNK-1 epitope ; glucuronyltransferase (GlcAT) ; asialo-orosomucoid (ASOR) ; branch specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The acceptor specificity of a rat brain glucuronyltransferase, GlcAT-P, associated with biosynthesis of the HNK-1 epitope on glycoproteins, was investigated using asialoorosomucoid as a model acceptor substrate. Structural analysis of N-linked oligosaccharides, to which glucuronic acid was transferred by GlcAT-P, by means of two-dimensional mapping of pyridylamino-oligosaccharides and MS spectrometry, demonstrated that the enzyme transferred glucuronic acid to bi-, tri-, and tetra-antennary complex type sugar chains, with almost equal efficiency, indicating that the enzyme has no preference as to the number of acceptor sugar branches. Next, we studied the branch specificity of this enzyme by means of the selective branch scission method involving two step exoglycosidase digestion using authentic pyridylamino-oligosaccharides. The GlcAT-P is highly specific for the terminal N-acetyllactosamine structure and no glucuronic acid was incorporated into a Galβ1-3GlcNAc moiety. The GlcAT-P transferred glucuronic acid to the galactose residues in the N-acetyllactosamine branches of bi-, tri-, and tetra-antennary oligosaccharide chains, with different efficiencies and most preferentially to those in the Galβ1-4GlcNAcβ1-4Manα1-3 branch.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1010973330152
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  • 9
    Electronic Resource
    Electronic Resource
    Regulation of biosynthesis ofN-glycolylneuraminic acid-containing glycoconjugates: characterization of factors required for NADH-dependent cytidine 5′monophosphate-N-acetylneuraminic acid hydroxylation (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 109-115 
    Details
    ISSN: 1573-4986
    Keywords: CMP-NeuAc hydroxylase ; N-glycolylneuraminic acid ; H-D antigen ; cytochromeb 5
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The hydroxylation of CMP-NeuAc has been demonstrated to be carried out by several factors including the soluble form of cytochromeb 5. In the present study, mouse liver cytosol was subjected to ammonium sulfate fractionation and cellulose phosphate column chromatography for the separation of two other essential fractions participating in the hydroxylation. One of the fractions, which bound to a cellulose phosphate column, was able to reduce the soluble cytochromeb 5, using NADH as an electron donor. The other fraction, which flowed through the column, was assumed to contain the terminal enzyme which accepts electrons from cytochromeb 5, activates oxygen, and catalyses the hydroxylation of CMP-NeuAc. Assay conditions for the quantitative determination of the terminal enzyme were established, and the activity of the enzyme in several tissues of mouse and rat was measured. The level of the terminal enzyme activity is associated with the expression ofN-glycolylneuraminic acid in these tissues, indicating that the expression of the terminal enzyme possibly regulates the overall velocity of CMP-NeuAc hydroxylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731194
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  • 10
    Electronic Resource
    Electronic Resource
    Characterization of a glucuronyltransferase: neolactotetraosylceramide glucuronyltransferase from rat brain (1992)
    Springer
    Glycoconjugate journal 9 (1992), S. 307-314 
    Details
    ISSN: 1573-4986
    Keywords: glucuronyltransferase ; HNK-1 antigen ; rat brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The properties of a rat brain glucuronyltransferase, which is presumed to be associated with the biosynthesis of the HNK-1 epitope on sulfoglucuronyl glycolipids, are described. The enzyme required divalent cations for reaction, with maximal activity at 10mm Mn2+, and exhibited a dual optimum at pH 4–5 and pH 6 depending upon the buffer used, with the highest activity at pH 4.5 in MES buffer. This enzyme strictly recognized the Galβ1-4GlcNAc terminal structure, and was highly specific for neolacto (type 2) glycolipids as acceptor. The enzyme was localized specifically in the brain, and was barely detected in other issues, including the thymus, spleen, liver, kidney, lung, and sciatic nerve fibres. Phosphatidylinositol and phosphatidylserine increased the enzymatic reaction 4.4- and 2.3-fold, respectively, whereas phosphatidylcholine slightly decreased the rate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731091
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