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Wyszukujesz frazę "sulfane" wg kryterium: Temat

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    Wyświetlanie 1-6 z 6
    Tytuł:
    Plasma levels of total, free and protein bound thiols as well as sulfane sulfur in different age groups of rats
    Autorzy:
    Iciek, Małgorzata
    Chwatko, Grażyna
    Lorenc-Koci, Elżbieta
    Bald, Edward
    Włodek, Lidia
    Powiązania:
    https://bibliotekanauki.pl/articles/1041562.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    sulfane sulfur
    disulfides
    age
    thiols
    plasma
    Opis:
    The redox status of plasma thiols can be a diagnostic indicator of different pathological states. The aim of this study was to identify the age dependent changes in the plasma levels of total, free and protein bound glutathione, cysteine and homocysteine. The determination was conducted in plasma of three groups of rats: 1) young (3-month-old), 2) middle aged (19-month-old), and 3) old (31-month-old). Total levels of glutathione, cysteine and homocysteine and their respective free and protein-bound fractions decreased with age. The only exception was a rise in free homocysteine concentration in the middle group, which indicates a different pattern of transformations of this thiol in plasma. The drop in the level of protein-bound thiols suggests that the antioxidant capacity of plasma diminishes with age, which, consequently, leads to impaired protection of -SH groups through irreversible oxidation. The plasma sulfane sulfur level also declines with age, which means that aging is accompanied by inhibition of anaerobic sulfur metabolism.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 3; 815-824
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Is aldehyde dehydrogenase inhibited by sulfur compounds? In vitro and in vivo studies
    Autorzy:
    Iciek, Małgorzata
    Górny, Magdalena
    Bilska-Wilkosz, Anna
    Kowalczyk-Pachel, Danuta
    Powiązania:
    https://bibliotekanauki.pl/articles/1038534.pdf
    Data publikacji:
    2018
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    aldehyde dehydrogenase
    reactive sulfur species
    sulfane sulfur
    Opis:
    Aldehyde dehydrogenase (ALDH) catalyzes the critical step of ethanol metabolism, i.e. transformation of toxic acetaldehyde to acetic acid. It is a redox sensitive protein with the key Cys in its active site. Recently, it has been documented that activity of some proteins can be modified by sulfur-containing molecules called reactive sulfur species leading to the formation of hydro- persulfides. The aim of the present study was to examine whether ALDH activity can be modified in this way. Studies were performed in vitro using yeast ALDH and various reactive sulfur species, including Na2S, GSSH, K2Sx, Na2S2O3, and garlic-derived allyl sulfides. The effect of garlic-derived trisulfide on ALDH activity was also studied in vivo in the rat liver. The obtained results clearly demonstrated that ALDH could be regulated by sulfur species which inhibited its enzymatic activity. The results also suggested that not H2S but polysulfides or hydropersulfides were the oxidizing species responsible for this modification. This process was easily reversible by reducing agents. After the treatment with polysulfides or hydropersulfides the level of protein-bound sulfur increased, while the activity of the enzyme dramatically decreased. Moreover, the study demonstrated that ALDH activity was inhibited in vivo in the rat liver after garlic-derived trisulfide administration. This is the first study reporting the regulation of ALDH activity by sulfane sulfur species and the results suggest that it leads to the inhibition of the enzyme.
    Źródło:
    Acta Biochimica Polonica; 2018, 65, 1; 125-132
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Hydrogen Embrittlement of Welded Joint Made of Supermartensitic Stainless Steel in Environment Containing Sulfane
    Autorzy:
    Jonšta, P.
    Váňová, P.
    Brožová, S.
    Pustějovská, P.
    Sojka, J.
    Jonšta, Z.
    Ingaldi, M.
    Powiązania:
    https://bibliotekanauki.pl/articles/352649.pdf
    Data publikacji:
    2016
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    hydrogen embrittlement
    sulfane
    tensile test
    supermartensitic stainless steel
    weld joint
    Opis:
    The work is focused on evaluation of resistance of the welded joint made of supermartensitic 13Cr6Ni2.5Mo stainless steel to sulfide stress cracking. Testing method A and solution B in accordance with NACE TM 0177 were used. All the testing samples were ruptured in a very short time interval but welded joint samples were fractured primarily in the weld metal or in heat affected zone and not in the basic material. Material analysis of samples were made with use of a ZEISS NEOPHOT 32 light microscope and a JEOL 6490LV scanning electron microscope.
    Źródło:
    Archives of Metallurgy and Materials; 2016, 61, 2A; 709-712
    1733-3490
    Pojawia się w:
    Archives of Metallurgy and Materials
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Menadione effect on l-cysteine desulfuration in U373 cells
    Autorzy:
    Wróbel, Maria
    Jurkowska, Halina
    Powiązania:
    https://bibliotekanauki.pl/articles/1041097.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    menadione
    astrocytoma U373
    sulfane sulfur
    3-mercaptopyruvate sulfurtransferase
    reactive oxygen species
    rhodanese
    Opis:
    The non-cytotoxic concentration (20 µM) of menadione (2-methyl-1,4-naphthoquinone), after 1 h of incubation, leads to loss of the activity of rhodanese by 33%, 3-mercaptopyruvate sulfurtransferase by 20%, as well as the level of sulfane sulfur by about 23% and glutathione by 12%, in the culture of U373 cells, in comparison with the control culture. Reactive oxygen species generated by menadione oxidize sulfhydryl groups in active centers of the investigated enzymes, inhibiting them and saving cysteine for glutathione synthesis. A decreased sulfane sulfur level can be correlated with an oxidative stress.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 2; 407-411
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Hydrogen sulfide generation from l-cysteine in the human glioblastoma-astrocytoma U-87 MG and neuroblastoma SHSY5Y cell lines
    Autorzy:
    Bronowicka-Adamska, Patrycja
    Bentke, Anna
    Wróbel, Maria
    Powiązania:
    https://bibliotekanauki.pl/articles/1038702.pdf
    Data publikacji:
    2017
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cystathionine
    beta-synthase
    gamma-cystathionase
    glutathione
    hydrogen sulfide
    3-mercaptopyruvate sulfurtransferase
    sulfane sulfur
    Opis:
    Hydrogen sulfide (H2S) is endogenously synthesized from l-cysteine in reactions catalyzed by cystathionine beta-synthase (CBS, EC 4.2.1.22) and gamma-cystathionase (CSE, EC 4.4.1.1). The role of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) in H2S generation is also considered; it could be important for tissues with low CTH activity, e.g. cells of the nervous system. The expression and activity of CBS, CTH, and MPST were detected in the human glioblastoma-astrocytoma (U-87 MG) and neuroblastoma (SHSY5Y) cell lines. In both cell lines, the expression and activity of MPST were the highest among the investigated enzymes, suggesting its possible role in the generation of H2S. The RP-HPLC method was used to determine the concentration of cystathionine and alpha-ketobutyrate, products of the CBS- and CTH-catalyzed reactions. The difference in cystathionine levels between cell homogenates treated with totally CTH-inhibiting concentrations of dl-propargylglycine and without the inhibitor was used to evaluate the activity of CBS. The higher expression and activity of CBS, CTH and MPST in the neuroblastoma cells were associated with more intensive generation of H2S in the presence of 2 mM cysteine. A threefold higher level of sulfane sulfur, a potential source of hydrogen sulfide, was detected in the astrocytoma cells in comparison to the neuroblastoma cells.
    Źródło:
    Acta Biochimica Polonica; 2017, 64, 1; 171-176
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The γ-glutamyltransferase activity and non-protein sulfhydryl compounds levels in rat kidney of different age groups.
    Autorzy:
    Włodek, Przemysław
    Sokołowska, Maria
    Smoleński, Olgierd
    Włodek, Lidia
    Powiązania:
    https://bibliotekanauki.pl/articles/1043788.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    L-cysteine
    kidney
    aging
    γ-glutamyl transferase
    reactive oxygen species
    protein-bound cysteine
    glutathione
    sulfane sulfur compounds
    Opis:
    The present work was aimed to obtain information about age-dependent changes of γ-glutamyltransferase (GGT) activity and the levels of non-protein sulfhydryl compounds (NPSH) in rat kidneys. In addition, protein-bound cysteine (PB-Cys), sulfane sulfur compounds and reactive oxygen species (ROS) were estimated The results indicate that the activity of GGT and NPSH levels in the kidneys are reduced with age. At the same time, a significant increase in the level of protein-bound cysteine was observed. Simultaneously, the content of sulfane sulfur compounds was increased in the group of the oldest animals. These findings indicate that the capacity for extracellular glutathione degradation and, in consequence, the availability of cysteine for intracellular glutathione biosynthesis may be impaired. The increased PB-Cys level indicates potentiation of the thiolation reaction, i.e. development of protein-mixed disulfides. These results reveal age dependent disturbances in the thiol-disulfide equilibrium in the kidneys which leads to an imbalance between pro- and antioxidatory processes.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 2; 501-507
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-6 z 6

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