Wynik wyszukiwania w bazie Polska Bibliografia Lekarska GBL

Zapytanie: WAŁAJTYS-RODE
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Tytuł oryginału: Effect of cyclosporin A on immunological response in lungs of guinea pigs infected with Trichinella spiralis.
Autorzy: Dzik Jolanta M., Zieliński Zbigniew, Gołos Barbara, Jagielska Elżbieta, Wranicz Mariusz, Wałajtys-Rode Elżbieta
Źródło: Acta Bioch. Pol. 2002: 49 (1) s.233-247, il., tab., bibliogr. s. 243-247 - 8 Międzynarodowe Sympozjum pt. Aspekty molekularne chemioterapii Gdańsk 09. 2001
Sygnatura GBL: 303,116

Hasła klasyfikacyjne GBL:
  • immunologia
  • mikrobiologia
  • farmacja
  • pulmonologia

    Typ dokumentu:
  • praca związana ze zjazdem
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • zwierzęta
  • Świnki morskie

    Streszczenie angielskie: The efects of cyclospirin A (CsA), a potent immunosuppressive drug with antiparasitic activity, on the innate immunological response in guinea pig lungs during an early period (6th adn 14th days) after T. spiralis infection were studied. CsA treatment of T. spiralis-infected guinea pigs caused a significant attenuation of immunological response in lungs by decreasing lymphocyte infiltration into pulmonary alveolar space, inhibiting alveolar macrophage superoxide anion production and lowering both the production of NO metabolites measured in bronchoalveolar lavage fluid and expression of the iNOS protein in lung homogenates, allowing us to speculate that the T. spiralis-dependent immunological reponse is dependent on lymphocyte T function. Interestingly, CsA itself had a pro-inflammatory effect, promoting leucotyte accumulation and macrophage superoxide production in guinea pig lungs. This observation may have a relevance to the situation in patients undergoing CsA therapy. Macrophage expression of the iNOS protein, evaluated by immunoblotting was not influenced by treatment of animals with CsA or anti-TGF-antibody, indicating different of the guinea pig and murine enzymes.

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    Tytuł oryginału: The effect of Arg209 to Lys mutation in mouse thymidylate synthase.
    Autorzy: Cieśla Joanna, Gołos Barbara, Wałajtys-Rode Elżbieta, Jagielska Elżbieta, Płucienniczak Andrzej, Rode Wojciech
    Źródło: Acta Bioch. Pol. 2002: 49 (3) s.651-658, il., tab., bibliogr. s. 657-658
    Sygnatura GBL: 303,116

    Hasła klasyfikacyjne GBL:
  • genetyka
  • onkologia
  • hematologia
  • mikrobiologia

    Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • zwierzęta
  • myszy

    Streszczenie angielskie: Mouse thymidylate synthase R209K (a mutation corresponding to R218K in Lactobacillus casei), overexpressed in thymidylate synthase-deficient Escherichia coli strain, was poorly soluble and with only feeble enzyme activity. The mutated protein, incubated with FdUMP and N5,10 -methylenetetrahydrofolate, did not form a complex stable under conditions of SDS/polyacrylamide gel electrophoresis. The reaction catalyzed by the R209K enzyme (studied in a crude extract), compared to that catalyzed by purified wild-type recombinant mouse thymidylate synthase, showed the Km value for dUMP 571-fold higher and Vmax value over 50-fold (assuming that the mutated enzyme constituted 20 p.c. of total crude extract protein) lower. Thus the ratios kcat, R209K/kcat, 'wild' and (kcat, R209K/Km, R209K**dUMP)/(kcat, 'wild'/Km, 'wild'**dUMP) were 0.019 and 0.000032, respectively, documenting that mouse thymidylate synthase R209, similar to the corresponding L. casei R218, is essential for both dUMP binding and enzyme reaction.

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