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  • Middle ear  (3)
  • (Nicotiana tabacum)  (1)
  • 3-epi-astrahygrol  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Nucleotide sequence of the PR-1 gene of Nicotiana tabacum
    Amsterdam : Elsevier
    FEBS Letters 225 (1987), S. 243-246 
    Details
    ISSN: 0014-5793
    Schlagwort(e): (Nicotiana tabacum) ; Genomic cloning ; PR1a gene ; Pathogenesis-related protein ; Pseudogene
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)81166-3
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  • 2
    Digitale Medien
    Digitale Medien
    Three triterpenes from Astraeus hygrometricus
    Amsterdam : Elsevier
    Phytochemistry 26 (1987), S. 2341-2344 
    Details
    ISSN: 0031-9422
    Schlagwort(e): 3-epi-astrahygrol ; Astraeus hygrometricus ; Astrahygrol ; Basidiomyces ; astrahygrone. ; higher fungi ; triterpenoids
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0031-9422(00)84715-9
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  • 3
    Digitale Medien
    Digitale Medien
    Cell-surface glycoconjugate layer in the tubotympanic mucosa of the guinea pig as revealed by wheat germ agglutinin/gold labelling (1995)
    Springer
    European archives of oto-rhino-laryngology and head & neck 252 (1995), S. 249-254 
    Details
    ISSN: 1434-4726
    Schlagwort(e): Middle ear ; Glycoconjugate ; Wheat germ agglutinin ; Electron microscopy ; Guinea pig
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract To evaluate the protective function of the mucous blanket (MB) against lectin substances, we examined at the ultrastructural level whether intraluminal colloidal gold-labelled wheat germ agglutinin (WGA) could enter the MB-covered epithelial cell surface of the guinea pig tubotympanic mucosa. Post-embedding staining with WGA/gold on thin tissue sections was done in parallel for comparison. The cell surface glycoconjugate of the eustachian tubal and transitional epithelium had a typical bilayered structure: the outer MB and the microvilli-associated glycocalyx (MAG), which were interposed by the interciliary fluid zone. In squamous epithelium of the distal middle ear, the MB adhered to the MAG, thereby forming a monolayered coat of glycoconjugates at the cell surface. In the pre-embedding staining, WGA/gold did not bind with the MB and MAG in the eustachian tube, and exclusively bound with MB in the transitional area. Direct binding was also found with MAG and the apical plasmic membrane in the squamous epithelium. These findings indicate that MAG is occluded by MB lined with the interciliary fluid zone for luminal access of lectin at the proximal lumina of the tubotympanic epithelium. It is also suggested that MB existing at two sites possesses a different WGA-binding capacity: shielding as a “dust cover” in the eustachian tube and entrapping as a “flypaper” against lectin in the transitional area of the middle ear.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00179920
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  • 4
    Digitale Medien
    Digitale Medien
    Sugar-binding sites with specificity for glucosamine in the guinea pig middle ear mucosa (1993)
    Springer
    European archives of oto-rhino-laryngology and head & neck 250 (1993), S. 412-417 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00180388
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  • 5
    Digitale Medien
    Digitale Medien
    Glycoconjugate histochemistry in the glycocalyx of guinea pig middle ear mucosa (1990)
    Springer
    European archives of oto-rhino-laryngology and head & neck 247 (1990), S. 291-295 
    Details
    ISSN: 1434-4726
    Schlagwort(e): Middle ear ; Lectin ; Glycocalyx
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary An attempt was made to determine the composition of oligosaccharide side chains in the apical cell surface glycocalices of the middle ear epithelium. This glycoconjugate is located on the innermost luminal surface, but its function is still unknown. The lectins evaluated included Triticum vulgare, Canavalia ensiformis, Maclura pomifera, Arachis hypogaea, Ricinus communis I (RCA-I), and Limax flavus. The staining results obtained with the six different lectin probes in the Lowicryl K4M-embedded guinea pig middle ear mucosa suggest that the glycocalyx contains β-d-N-acetylglucosamine, sialic acid, and β-d-galactose in the major carbohydrate moiety. The present study also indicates that a polarity exists on the cell surfaces in the distribution pattern of the carbohydrate component, especially those of β-galactosyl residues, as revealed by RCA-I binding. This may imply functional separation of the epithelial cells.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00176540
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