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    Wyświetlanie 1-6 z 6
    Tytuł:
    Aldolase A is present in smooth muscle cell nuclei
    Autorzy:
    Mamczur, Piotr
    Dzugaj, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1040689.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    aldolase
    nucleus
    heterochromatin
    smooth muscle
    isoenzymes
    Opis:
    Previously we have shown that aldolase (ALD; EC 4.1.2.13) is present in cardiomyocyte nuclei. Now, we focused our attention on ALD localization in smooth muscle cells. Immunocytochemical methods were used to study the subcellular localization of ALD. Aldolase was localized in the cytoplasm as well as in the nuclei. Within the nuclei ALD was located in the heterochromatin region. Native polyacrylamide gel electrophoresis followed by aldolase activity staining in gel was used to study the ALD isoenzyme pattern in porcine smooth muscle cells. Two ALD isoenzymes, A and C, were found in these cells but in the nuclei only the muscle isoenzyme was detected. To support the nuclear localization of ALD, measurement of aldolase activity in the smooth muscle cell nuclei isolated from porcine stomach was performed. The ALD activity in the isolated nuclei was detectable only after preincubation of the nuclear fraction with Triton X-100 and high concentration of KCl.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 799-805
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Fluorescence investigations on the interaction of rabbit liver D-fructose-1,6-bisphosphate 1-phosphohydrolase with bovine serum albumin
    Autorzy:
    Dżugaj, Andrzej
    Gancarz, Roman
    Powiązania:
    https://bibliotekanauki.pl/articles/1045753.pdf
    Data publikacji:
    1990
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Źródło:
    Acta Biochimica Polonica; 1990, 37, 4; 433-444
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Rabbit muscle fructose-1,6-bisphosphatase is phosphorylated in vivo.
    Autorzy:
    Rakus, Dariusz
    Zarzycki, Marek
    Dzugaj, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1043652.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    aldolase
    muscle
    phosphorylation
    AMP
    fructose-1,6-bisphosphatase
    Opis:
    Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like Km and kcat, which are two times higher for the phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. ephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 1; 115-121
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Życie i tragiczna śmierć Jakuba Karola Parnasa, wybitnego polskiego biochemika, współodkrywcy glikolizy
    The life and tragic death of Jakub Karol Parnas, a prominent polish biochemist, co-discoverer of glycolysis
    Autorzy:
    Barańska, Jolanta
    Dżugaj, Andrzej
    Kwiatkowska-Korczak, Janina
    Powiązania:
    https://bibliotekanauki.pl/articles/1197507.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Przyrodników im. Kopernika
    Opis:
    The contribution of Jakub Karol Parnas (1884-1949), a prominent Polish scientist, to the understanding of muscle biochemistry, including ammonia and carbohydrates sources and nucleotide metabolism, is described. Among his main achievements was the discovery of glycogen phosphorolysis, the first use of radioactive phosphorus in biological studies, and formulation and proof of phosphate transfer between glycolytic intermediates and ATP. The rewarding and successful life led by this man of great scientific and intellectual abilities up to the beginning of the Second World War, his dramatic fate during the war, and his tragic death in a Soviet prison reflects the turbulent 20th history of the region.
    Źródło:
    Kosmos; 2008, 57, 1-2; 1-17
    0023-4249
    Pojawia się w:
    Kosmos
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Regulation of subcellular localization of muscle FBPase in cardiomyocytes. The decisive role of calcium ions
    Autorzy:
    Majkowski, Michal
    Wypych, Dorota
    Pomorski, Pawel
    Dzugaj, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1042732.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cardiomyocytes
    Z-line
    insulin
    calcium
    intercalated disc
    muscle FBPase
    Opis:
    Glyconeogenesis, the synthesis of glycogen from carbohydrate precursors like lactate, seems to be an important pathway participating in replenishing glycogen in cardiomyocytes. Fructose-1,6-bisphosphatase (FBPase), an indispensible enzyme of glyconeogenesis, has been found in cardiomyocytes on the Z-line, in the nuclei and in the intercalated discs. Glyconeogenesis may proceed only when FBPase accumulates on the Z-line. Searching for the mechanism of a FBPase regulation we investigated the effects of the calcium ionophore A23187, a muscle relaxant dantrolene, glucagon, insulin and medium without glucose on the subcellular localization of this enzyme in primary culture of neonatal rat cardiomyocytes. Immunofluorescence was used for protein localization and the intracellular calcium concentration was measured with Fura. We found that the concentration of calcium ions was the decisive factor determining the localization of muscle FBPase on the Z-line. Calcium ions had no effect on the localization of the enzyme in the intercalated discs or in the nuclei, but accumulation of FBPase in the nuclei was induced by insulin.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 4; 597-605
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-6 z 6

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