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Zapytanie: KREMSER
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Tytuł oryginału: The structure of the oligosaccharides of ŕ3á1 integrin from human ureter epithelium (HCV29) cell line.
Autorzy: Lityńska Anna, Pocheć Ewa, Hoja-Łukowicz Dorota, Kremser Elżbieta, Laidler Piotr, Amoresano Angela, Monti Chiara
Źródło: Acta Bioch. Pol. 2002: 49 (2) s.491-500, il., tab., bibliogr. s. 499-500
Sygnatura GBL: 303,116

Hasła klasyfikacyjne GBL:
  • urologia

    Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • ludzie
  • in vitro

    Streszczenie angielskie: There is a growing line of evidence that glycosylation of ŕ and á subunits is important for the function of integrins. Integrin ŕ3á1, from human ureter epithelium cell - line HCV29, was isolated by affinity chromatography on laminin GD6 peptide. Characterization of its carbohydrate moieties was carried out using sodium dodecyl sulfate/polyacrylamide gel electrophoresis followed by Western blotting on Immobilon P and on-blot deglycosylation with peptide N-glycosidase-F. Profiles of N-glycans for each subunit were obtained by matrix-assisted laser desorption/ionization mass spectrometry. Our findings demonstrated, in both subunits of integrin ŕ3á1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi-tri- and tetraantennary structures were the most common, while hig-mannose type structures were minor. Also the presence of short poly-N-acetyllactosamine entities was shown. These results show that while tha predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.

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