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  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 1190 (1994), S. 297-303 
    ISSN: 0005-2736
    Schlagwort(e): Band 3 ; Diamide ; Erythrocyte ; Erythrocyte removal ; Oxidative damage ; Phagocytosis
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Medizin , Physik
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    ISSN: 1573-4986
    Schlagwort(e): β1 ; 4-N-acetylgalactosaminyltransferase ; Sda blood-group antigen ; CaCo-2 cells ; enterocyte differentiation ; polarized release
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract We have previously shown that human colon carcinoma CaCo-2 cells express the Sda-β1,4-N-acetylgalactosaminyltransferase (Sda-βGalNAc-transferase) and that the enzyme activity correlates with the degree of enterocytic differentiation. Here we report that a large amount of this glycosyltransferase is released in soluble form, particularly when CaCo-2 cells are maintained in culture for more than 3 weeks in order to ensure an higher degree of enterocyte differentiation. The soluble enzyme was concentrated and partially purified by Blue-Sepharose and fetuin-Sepharose chromatography. The substrate specificity of the partially purified enzyme was similar to that of Sda-enzyme from epithelial cells of colon mucosa, and for its activity strictly required the presence in acceptors of NeuAc in α2,3-linkage to subterminal galactose. Among the low molecular glycans tested, NeuAcα2,3Galβ1,4GlcNAc appeared to be the best acceptor, whereas sialyl-Lewisx and sialyl-Lewisa did not serve as acceptors, indicating that the fucosylation of sub-terminal GlcNAc hindered the transferase activity. Contrary to this, the activity towards a disialylated acceptor such as di-sialyl-lacto-N-tetraose was reduced but not abolished. When CaCo-2 cells were cultured on porous membranes and the transferase activity assayed in medium collected from chambers corresponding to either the apical or basolateral face of highly differentiated CaCo-2 cells, a preferential release from the basolateral surface was found. Considering that Sda-βGalNAc-transferase is mainly located in the large intestine, current results support the notion that colonic cells largely contribute to the presence of the enzyme in human plasma.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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