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  • 1980-1984  (4)
  • 1905-1909
  • 1890-1899
  • extracellular materials  (2)
  • Ausbrand  (1)
  • Biloma  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Abdominal imaging 9 (1984), S. 213-217 
    ISSN: 1432-0509
    Schlagwort(e): Biliary ascites ; Biloma ; Intraperitoneal fluid, differentiation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Free or loculate intraperitoneal fluid can easily be detected by ultrasonography or computerized tomography. The differentiation of bile fluid from other liquid collections and the documentation of the presence and extent of a bile leak can be difficult diagnostic problems. In representative case studies the use and the diagnostic limits of ultrasonography and CT in the diagnosis of intraperitoneal bile accumulations are discussed. A diagnostic algorithm including cholescintigraphy for the evaluation of biliary leakage is proposed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Chemie Ingenieur Technik - CIT 56 (1984), S. 550-551 
    ISSN: 0009-286X
    Schlagwort(e): Wirbelschicht-Feuerung ; Feststoffverweilzeit ; Kokspartikeln ; Ausbrand ; Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 13 (1980), S. 219-227 
    ISSN: 0091-7419
    Schlagwort(e): lectins ; lectin binding sites ; cell surfaces ; extracellular materials ; Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: A lactose-binding lectin previously purified from embryonic chicken muscle and adult chicken liver, and here referred to as chicken-lactose-lectin-I (CLL-I), was added to sections of various adult chicken tissues to detect available binding sites. Both the sites of binding of added CLL-I as well as the tissue distribution of endogenous CLL-I were determined by indirect immunofluorescence using a rabbit antibody to CLL-I followed by fluorescent goat anti-rabbit IgG. Some tissues such as intestine and kidney showed abundant extracellular binding sites for the lectin, primarily between cells, in basement membrane, and in material on the luminal surface. In contrast, adult heart showed no significant binding sites for CLL-I. Adult pancreas showed considerable endogenous CLL-I in an extracellular site surrounding exocrine lobules, but added CLL-I did not bind substantially. The distribution of CLL-I binding sites in intestine were mimicked by those of purpurin, another lactose-binding lectin. CLL-I binding sites were also detected on the surface of cultured chick embryo skin fibroblasts. The factors controlling the specific distribution of occupied and unoccupied CLL-I binding sites are not known.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 16 (1981), S. 233-242 
    ISSN: 0275-3723
    Schlagwort(e): lectins ; slime mold lectins ; vertebrate lectins ; chicken-lactose-lectin-I ; chicken-lactose-lectin-II ; chicken heparin lectin ; Dictyostelium ; secretion ; muscle development ; extracellular materials ; Chemistry ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Endogenous lectins in both cellular slime molds and chicken tissues have been localized primarily intracellularly, in contrast with the predominantly extracellular localization of the glycoproteins, glycolipids, and glycosaminoglycans with which they might interact. Here we present evidence that lectins in both of these organisms may be externalized and become associated with the cell surface and/or extracellular materials. In chicken intestine, chicken-lactose-lectin-II is shown to be localized in the secretory granules of the goblet cells, along with mucin, and to be secreted onto the intestinal surface. In embryonic muscle, chicken-lactose-lectin-I is shown to be externalized with differentiation, ultimately becoming localized on the surface of myotubes and in the extracellular spaces. In a cellular slime mold, Dictyostelium purpureum, externalization of lectin is elicited by either polyvalent glycoproteins that bind the small amount of endogenous cell surface lectin, or by slime mold or plant lectins that bind unoccupied complementary cell surface oligosaccharides. These results suggest that externalization of endogenous lectin may be a response to specific external signals. We conclude that lectins are frequently held in intracellular reserves awaiting release for specific external functions.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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