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  • 1
    Electronic Resource
    Electronic Resource
    Structural requirements for the binding of oligosaccharides to immobilized lectin ofErythrina variegata (Linn) var.Orientalis (1990)
    Springer
    Glycoconjugate journal 7 (1990), S. 311-322 
    Details
    ISSN: 1573-4986
    Keywords: oligosaccharide binding ; immobilized lectin ; Erythrina
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins withErythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100°C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Galβ1-4GlcNAcβ1-3(Galβ1-4GlcNAcβ1-6)Gal sugar sequence, which is an l-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01073375
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  • 2
    Electronic Resource
    Electronic Resource
    cDNA cloning of mouse VLA-3 α subunit (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 57 (1995), S. 371-377 
    Details
    ISSN: 0730-2312
    Keywords: integrin ; VLA (very late antigen) ; adhesion molecule ; cDNA cloning ; tissue distribution ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: cDNA clones for mouse VLA (very late antigen)-3 α subunit (α3 integrin) were isolated and sequenced. The encoded mouse α3 integrin subunit was composed of 1,053 amino acid residues. The results of sequence analysis revealed similar structural characteristics to other VLA α subunits. For example, the presence of a large extracellular domain including three putative metal binding sequences, a transmembrane domain, and a short cytoplasmic domain. A higher level of its message was detected in thymus than in kidney, stomach, spleen, liver, brain, or lung by Northern blotting analysis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240570221
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