Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "Szewczyk, Adam." wg kryterium: Autor

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-8 z 8
    Tytuł:
    Transmembrane segment M2 of glycine receptor as a model system for the pore-forming structure of ion channels.
    Autorzy:
    Bednarczyk, Piotr
    Szewczyk, Adam
    Dołowy, Krzysztof
    Powiązania:
    https://bibliotekanauki.pl/articles/1043689.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    black lipid membrane
    ion channels
    glycine receptor
    Opis:
    The glycine receptor belongs to the ligand-gated ion channel superfamily. It is a chloride conducting channel composed of four transmembrane domains. It was previously shown that the second transmembrane domain (M2) of the glycine receptor forms an ion conduction pathway throught lipid bilayers. The amino-acid sequence of the transmembrane segment M2 of the glycine receptor has a high homology to all receptors of the ligand-gated ion channel superfamily. In our report, we have used a synthetic M2 peptide. It was incorporated into a planar membrane of known lipid composition and currents induced by M2 were measured by the Black Lipid Membrane technique. When the planar lipid bilayer was composed of 75% phosphatidylethanolamine and 25% phosphatidylserine, the reversal potential measured in a 150/600 mM KCl (cis/trans) gradient was -19 mV suggesting that the examined pore was preferential to anions, PK/PCl = 0.25. In contrast, when 75% phosphatidylserine and 25% phosphatidylethanolamine was used, the reversal potential was +20 mV and the pore was preferential to cations, PK/PCl = 4.36. Single-channel currents were recorded with two predominant amplitudes corresponding to the main-conductance and sub-conductance states. Both conductance states (about 12 pS and 30 pS) were measured in a symmetric solution of 50 mM KCl. The observed single-channel properties suggest that the selectivity and conductance of the pore formed by the M2 peptide of the glycine receptor depend on the lipid composition of the planar bilayer.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 4; 869-875
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Benzodiazepine binding to mitochondrial membranes of the amoeba Acanthamoeba castellanii and the yeast Saccharomyces cerevisiae.
    Autorzy:
    Slocinska, Malgorzata
    Szewczyk, Adam
    Hryniewiecka, Lilla
    Kmita, Hanna
    Powiązania:
    https://bibliotekanauki.pl/articles/1041507.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Saccharomyces cerevisiae
    Acathamoeba castellanii
    Ro5-4864
    mitochondrial benzodiazepine receptor
    Opis:
    Benzodiazepine binding sites were studied in mitochondria of unicellular eukaryotes, the amoeba Acathamoeba castellanii and the yeast Saccharomyces cerevisiae, and also in rat liver mitochondria as a control. For that purpose we applied Ro5-4864, a well-known ligand of the mitochondrial benzodiazepine receptor (MBR) present in mammalian mitochondria. The levels of specific [3H]Ro5-4864 binding, the dissociation constant (KD) and the number of [3H]Ro5-4864 binding sites (Bmax) determined for fractions of the studied mitochondria indicate the presence of specific [3H]Ro5-4864 binding sites in the outer membrane of yeast and amoeba mitochondria as well as in yeast mitoplasts. Thus, A. castellanii and S. cerevisiae mitochondria, like rat liver mitochondria, contain proteins able to bind specifically [3H]Ro5-4864. Labeling of amoeba, yeast and rat liver mitochondria with [3H]Ro5-4864 revealed proteins identified as the voltage dependent anion selective channel (VDAC) in the outer membrane and adenine nucleotide translocase (ANT) in the inner membrane. Therefore, the specific MBR ligand binding is not confined only to mammalian mitochondria and is more widespread within the eukaryotic world. However, it can not be excluded that MBR ligand binding sites are exploited efficiently only by higher multicellular eukaryotes. Nevertheless, the MBR ligand binding sites in mitochondria of lower eukaryotes can be applied as useful models in studies on mammalian MBR.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 4; 953-962
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Intracellular potassium and chloride channels: An update.
    Autorzy:
    Dębska, Grażyna
    Kicińska, Anna
    Skalska, Jolanta
    Szewczyk, Adam
    Powiązania:
    https://bibliotekanauki.pl/articles/1044174.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    ATP
    ion channels
    chromaffin granules
    mitochondria
    chloride channel
    potassium channel openers
    sulfonylurea
    Opis:
    Channels selective for potassium or chloride ions are present in all intracellular membranes such as mitochondrial membranes, sarcoplasmic/endoplasmic reticulum, nuclear membrane and chromaffin granule membranes. They probably play an important role in events such as acidification of intracellular compartments and regulation of organelle volume. Additionally, intracellular ion channels are targets for pharmacologically active compounds, e.g. mitochondrial potassium channels interact with potassium channel openers such as diazoxide. This review describes current observations concerning the properties and functional roles of intracellular potassium and chloride channels.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 1; 137-144
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Mitochondrial potassium and chloride channels.
    Autorzy:
    Kicińska, Anna
    Dębska, Grażyna
    Kunz, Wolfram
    Szewczyk, Adam
    Powiązania:
    https://bibliotekanauki.pl/articles/1044286.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    ATP
    ion channels
    mitochondria
    chloride channel
    potassium channel
    channel openers
    sulfonylurea
    Opis:
    Channels selective for potassium or chloride ions are present in inner mitochondrial membranes. They probably play an important role in mitochondrial events such as the formation of ΔpH and regulation of mitochondrial volume changes. Mitochondrial potassium and chloride channels could also be the targets for pharmacologically active compounds such as potassium channel openers and antidiabetic sulfonylureas. This review describes the properties, pharmacology, and current observations concerning the functional role of mitochondrial potassium and chloride channels.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 3; 541-551
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Does the energy state of mitochondria influence the surface potential of the inner mitochondrial membrane? A critical appraisal
    Autorzy:
    Wojtczak, Lech
    Nałęcz, Maciej
    Famulski, Konrad
    Dygas, Anna
    Szewczyk, Adam
    Powiązania:
    https://bibliotekanauki.pl/articles/1045919.pdf
    Data publikacji:
    1987
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Źródło:
    Acta Biochimica Polonica; 1987, 34, 3; 299-318
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-8 z 8

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies