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Wyświetlanie 1-4 z 4
Tytuł:
Modulation of FAD-dependent monooxygenase activity from aromatic compounds-degrading Stenotrophomonas maltophilia strain KB2
Autorzy:
Wojcieszyńska, Danuta
Greń, Izabela
Hupert-Kocurek, Katarzyna
Guzik, Urszula
Powiązania:
https://bibliotekanauki.pl/articles/1039898.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
phenols
monooxygenase
inhibitors
Stenotrophomonas
Opis:
The purpose of this study was purification and characterization of phenol monooxygenase from Stenotrophomonas maltophilia strain KB2, enzyme that catabolises phenol and its derivatives through the initial hydroxylation to catechols. The enzyme requires NADH and FAD as a cofactors for activity, catalyses hydroxylation of a wide range of monocyclic phenols, aromatic acids and dihydroxylated derivatives of benzene except for catechol. High activity of this monooxygenase was observed in cell extract of strain KB2 grown on phenol, 2-methylphenol, 3-metylphenol or 4-methylphenol. Ionic surfactants as well as cytochrome P450 inhibitors or 1,4-dioxane, acetone and n-butyl acetate inhibited the enzyme activity, while non-ionic surfactants, chloroethane, ethylbenzene, ethyl acetate, cyclohexane, and benzene enhanced it. These results indicate that the phenol monooxygenase from Stenotrophomonas maltophilia strain KB2 holds great potential for bioremediation.
Źródło:
Acta Biochimica Polonica; 2011, 58, 3; 421-426
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Characterization of DNA sequences localized 11 to 17.5 kb upstream of the chicken embryonic π-globin gene
Autorzy:
Pietrowska, Monika
Rusin, Marek
Widłak, Piotr
Razin, Sergey
Rzeszowska-Wolny, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1044491.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1999, 46, 3; 777-784
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Inhibitors of benzamidine type influence the virulence properties of Porphyromonas gingivalis strains.
Autorzy:
Eick, Sigrun
Pfister, Wolfgang
Stürzebecher, Uta
Jarema, Sigrid
Stürzebecher, Jörg
Powiązania:
https://bibliotekanauki.pl/articles/1043444.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Porphyromonas gingivalis strains
growth inhibition
inhibitors of benzamidine type
phagocytosis and intracellular killing
adhesion to KB cells
Opis:
Synthetic inhibitors of benzamidine type have been found to have inhibiting effects on arginine specific cysteine proteinases of P. gingivalis. The purpose of our study was to assess the effects of these inhibitors on the virulence properties of two P. gingivalis strains, the reference strain ATCC 33277 and JH16-1, a clinical isolate obtained from a patient with severe periodontitis. The inhibitors tested were pentamidine, benzamidine, three bis-benzamidine derivatives with a pentamidine-related structure, one bis-benzamidine derivative with another structure, and one arginine derivative as a negative control, each in the concentrations of 2 μM and 20 μM. As virulence criteria the following parameters were determined : arginine-specific amidolytic activity, growth inhibition, hemagglutination of sheep erythrocytes, adherence to KB cells and immuno-phagocytosis including intracellular killing. Pentamidine and the bis-benzamidine derivatives with pentamidine-related structure showed the most remarkable effects on reduction of amidolytic activity by 35%, growth inhibition and reduced hemagglutination. Except for the arginine derivative all other inhibitors tested enhanced the phagocytosis capacities of granulocytes. No clear influence of the inhibitors on adherence of P. gingivalis to KB cells was seen. Although in vitro effects of the synthetic inhibitors of cysteine proteinases on virulence of P. gingivalis were observed further in vitro tests concerning immunomodulatory effects should be done before these substances are used for therapy in clinically controlled studies.
Źródło:
Acta Biochimica Polonica; 2003, 50, 3; 725-734
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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