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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    European archives of oto-rhino-laryngology and head & neck 250 (1993), S. 412-417 
    ISSN: 1434-4726
    Schlagwort(e): Sugar-binding site ; Guinea pig ; Middle ear ; Lipopolysaccharide ; Electron microscopy
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary Glucosamine-binding sites were detected in Lowicryl K4M-embedded guinea pig middle ear mucosa by electron microscopy, using glucosaminyl bovine serum albumin. Incubation of ultrathin tissue sections with gold-labeled glucosaminyl bovine serum albumin (GlcN/BSA/gold) resulted in binding mainly on cilia, microvilli, rough endoplasmic reticulum and nuclei. The sugar binding was not inhibited after ultrathin sections had been digested with trypsin or neuraminidase. Various carbohydrates and glycoconjugates were tested as competitive inhibitors of G1cN/BSA/gold labeling on the tissue sections. The sugar specificity range detected by the glucosamine-binding sites included glucosamine, N-acetylglucosamine, mannose and fucose, whereas N-acetylgalactosamine, galactose and glucose were not detectable. A series of endotoxic substances such as Salmonella minnesota Re595 lipid A complex with BSA and lipopolysaccharides (LPS) derived from Escherichia coli 055: B5 or S. minnesota Re595 also competed with GlcN/BSA/gold binding. This indicates that the lipid A backbone glucosamine or other carbohydrate portions of LPS is a part of the structure recognized by glucosamine binding sites.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    European archives of oto-rhino-laryngology and head & neck 250 (1993), S. 337-341 
    ISSN: 1434-4726
    Schlagwort(e): N-Acetylglucosamine ; Sugar-binding site ; Middle ear mucosa ; Guinea pig
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The distribution of sugar-binding sites was analyzed in Lowicryl K4M-embedded guinea pig middle ear mucosa. Four neoglycoproteins and a glycoprotein were used as probes: N-acetyl-d-glucosamine (GlcNAc), d-mannose, N-acetyl-d-galactosamine, or l-fucose carrying bovine serum albumin (BSA) and asialofetuin with terminal d-galactosyl sugar residues. Each probe was then labelled with 15 nm colloidal gold. Incubation of ultrathin sections with gold-labelled p-aminophenyl N-acetyl-β-d-glucosaminide-BSA (GlcNAc/BSA/gold) led to binding on mucosal cilial, microvilli, rough endoplasmic reticulum, mitochondria, and nuclei. No binding occurred with asialofetuin or neoglycoproteins containing mannose, N-acetylgalactosamine or fucose. Various control experiments showed that specificity of G1cNAc/BSA/gold binding was directed towards N-acetylglucosaminyl residues expressed on the neoglycoprotein. Competitive sugar inhibition with GlcNAc and its derivatives suggested that the strong affinity for GlNAc-binding sites took place in a complex formation with sugar residues bound to a carrier protein. The existence of a hydrophobic region close to the sugar-binding site was also suggested.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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