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    Wyświetlanie 1-4 z 4
    Tytuł:
    Activity of superoxide dismutase obtained from senile cataract lens - effect of diabetes mellitus
    Autorzy:
    Panz, Tomasz
    Wójcik, Rafał
    Krukar-Baster, Krystyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1040692.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Cu,Zn superoxide dismutase activity
    senile cataract
    diabetes mellitus
    Opis:
    The activity of Cu,Zn superoxide dismutase in the fluid obtained from eye lens capsules after cataract surgery was investigated in samples obtained from patients with senile cataract and with senile cataract combined with diabetes mellitus. Two parameters were measured and compared: the frequency of occurrence of detected superoxide dismutase activity and the relative activity of the enzyme in samples derived from senile cataract patients versus those from the patiens affected additionally by diabetes mellitus. It was confirmed that the decrease of superoxide dismutase activity during cataract was additionally promoted by diabetes mellitus.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 821-823
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Zinc-binding proteins from boar seminal plasma - isolation, biochemical characteristics and influence on spermatozoa stored at 4°C
    Autorzy:
    Mogielnicka-Brzozowska, Marzena
    Wysocki, Paweł
    Strzeżek, Jerzy
    Kordan, Władysław
    Powiązania:
    https://bibliotekanauki.pl/articles/1039909.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    boar
    spermatozoa
    zinc
    Zn2+-binding proteins
    cold shock
    Opis:
    Affinity chromatography on Chelating Sepharose Fast Flow Gel-Zn2+ was used for fractionation of boar seminal plasma proteins. Approximately 30% of total boar seminal plasma proteins showed affinity for zinc ions (ZnBP fraction). Native electrophoresis (PAGE) of ZnBP revealed six protein fractions which separated into 27 bands under denaturing conditions (SDS/PAGE). Two-dimensional electrophoresis (2D PAGE) showed 148 polypeptides with isoelectric points mostly in the basic and neutral pH range. The zinc-binding proteins comprise mainly 10-20 kDa polypeptides which are probably members of the spermadhesin family. ZnBP present in the incubation mixture of spermatozoa stored for 1 or 24 h at 4 °C allowed preservation of a higher percentage of cells exhibiting linear motility in comparison to a control sample stored in PBS. Presented results indicate that proteins binding Zn2+ ions have a shielding effect on the sperm plasma membrane and acrosome of spermatozoa, protecting these structures against consequences of cold shock.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 2; 171-177
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Cu,Zn-superoxide dismutase deficiency in mice leads to organ-specific increase in oxidatively damaged DNA and NF-κB1 protein activity
    Autorzy:
    Siomek, Agnieszka
    Brzoska, Kamil
    Sochanowicz, Barbara
    Gackowski, Daniel
    Rozalski, Rafal
    Foksinski, Marek
    Zarakowska, Ewelina
    Szpila, Anna
    Guz, Jolanta
    Bartlomiejczyk, Teresa
    Kalinowski, Bartlomiej
    Kruszewski, Marcin
    Olinski, Ryszard
    Powiązania:
    https://bibliotekanauki.pl/articles/1042730.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Cu,Zn-SOD deficiency
    NF-κB pathway
    oxidative stress
    Opis:
    Earlier experimental studies have demonstrated that: i) Cu,Zn-superoxide dismutase deficiency leads to oxidative stress and carcinogenesis; ii) dysregulation of NF-κB pathway can mediate a wide variety of diseases, including cancer. Therefore, we decided, for the first time, to examine the level of oxidative DNA damage and the DNA binding activity of NF-κB proteins in SOD1 knockout, heterozygous and wild-type mice. Two kinds of biomarkers of oxidatively damaged DNA: urinary excretion of 8-oxodG and 8-oxoGua, and the level of oxidatively damaged DNA were analysed using HPLC-GC-MS and HPLC-EC. The DNA binding activity of p50 and p65 proteins in a nuclear extracts was assessed using NF-κB p50/p65 EZ-TFA transcription factor assay. These parameters were determined in the brain, liver, kidney and urine of SOD1 knockout, heterozygous and wild-type mice. The level of 8-oxodG in DNA was higher in the liver and kidney of knockout mice than in wild type. No differences were found in urinary excretion of 8-oxoGua and 8-oxodG between wild type and the SOD1-deficient animals. The activity of the p50 protein was higher in the kidneys, but surprisingly not in the livers of SOD1-deficient mice, whereas p65 activity did not show any variability. Our results indicate that in Cu,Zn-SOD-deficient animals the level of oxidative DNA damage and NF-κB1 activity are elevated in certain organs only, which may provide some explanation for organ-specific ROS-induced carcinogenesis.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 4; 577-583
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Heparin- and Zn^2+-binding proteins from boar seminal plasma
    Autorzy:
    Hołody, Dariusz
    Strzeżek, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044452.pdf
    Data publikacji:
    1999
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    boar seminal plasma
    heparin-binding proteins
    Zn^{2+}-binding proteins
    Opis:
    Low molecular mass, heparin-binding proteins from seminal plasma play an important role in gametes interaction whereas plasmatic Zn^{2+}-binding proteins stabilize chromatin and plasmalemma structures and protect spermatozoa in the female reproductive tract. By means of affinity chromatography the heparin- and Zn^{2+}-binding proteins were isolated from boar seminal plasma and both preparations were analyzed by reverse HPLC. Most of the proteins bound to heparine and Zn^{2+}-ions were classified as spermadhesins. Three fractions binding exclusively Zn^{2+} were isolated. They differ in amino-acid composition, content of glucosamine and content of protein components revealed by SDS/PAGE.
    Źródło:
    Acta Biochimica Polonica; 1999, 46, 4; 935-939
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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