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 "calcium-binding proteins" wg kryterium: Temat

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-5 z 5
    Tytuł:
    The influence of bilberry fruit on memory and the expression of parvalbumin in the rat hippocampus
    Autorzy:
    Borowiec, K.
    Matysek, M.
    Szwajgier, D.
    Biała, G.
    Kruk-Słomka, M.
    Szalak, R.
    Ziętek, J.
    Arciszewski, M.B.
    Targoński, Z.
    Powiązania:
    https://bibliotekanauki.pl/articles/2087496.pdf
    Data publikacji:
    2019
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    bilberry
    calcium-binding proteins
    hippocampus
    memory
    rat
    Źródło:
    Polish Journal of Veterinary Sciences; 2019, 3; 481-487
    1505-1773
    Pojawia się w:
    Polish Journal of Veterinary Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Calcium-binding calmyrin forms stable covalent dimers in vitro, but in vivo is found in monomeric form.
    Autorzy:
    Sobczak, Adam
    Blazejczyk, Magdalena
    Piszczek, Grzegorz
    Zhao, Gang
    Kuznicki, Jacek
    Wojda, Urszula
    Powiązania:
    https://bibliotekanauki.pl/articles/1041431.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    covalent dimer
    calmyrin monomer
    human lymphocytes
    EF-hand calcium-binding proteins
    Opis:
    The EF-hand Ca^(2+)-binding protein calmyrin is expressed in many tissues and can interact with multiple effector proteins, probably as a sensor transferring Ca^(2+) signals. As oligomerization may represent one of Ca^(2+)-signal transduction mechanisms, we characterised recombinant calmyrin forms using non-reducing SDS/PAGE, analytical ultracentrifugation and gel filtration. We also aimed at identification of biologically active calmyrin forms. Non-reducing SDS/PAGE showed that in vitro apo- and Ca^(2+)-bound calmyrin oligomerizes forming stable intermolecular disulfide bridges. Ultracentrifugation indicated that at a 220 µM initial protein concentration apo-calmyrin existed in an equilibrium of a 21.9 kDa monomer and a 43.8 kDa dimer (trimeric or tetrameric species were not detected). The dimerization constant was calculated as Ka = 1.78 × 103 M^(-1) at 6oC. Gel filtration of apo- and Ca^(2+)-bound calmyrin at a 100 µM protein concentration confirmed an equilibrium of a monomer and a covalent dimer state. Importantly, both monomer and dimer underwent significant conformational changes in response to binding of Ca^(2+). However, when calmyrin forms were analyzed under non-reducing conditions in cell extracts by Western blotting, only monomeric calmyrin was detected in human platelets and lymphocytes, and in rat brain. Moreover, in contrast to recombinant calmyrin, crosslinking did not preserve any dimeric species of calmyrin regardless of Ca^(2+) concentrations. In summary, our data indicate that although calmyrin forms stable covalent dimers in vitro, it most probably functions as a monomer in vivo.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 2; 469-476
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Ca2+differently affects hydrophobic properties of guanylyl cyclase-activating proteins (GCAPs) and recoverin.
    Autorzy:
    Gorczyca, Wojciech
    Kobiałka, Marcin
    Kuropatwa, Marianna
    Kurowska, Ewa
    Powiązania:
    https://bibliotekanauki.pl/articles/1043612.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    fluorescence
    calcium-binding proteins
    recoverin
    guanylyl cyclase-activating proteins
    Opis:
    Guanylyl cyclase-activating proteins (GCAPs) and recoverin are retina-specific Ca2+-binding proteins involved in phototransduction. We provide here evidence that in spite of structural similarities GCAPs and recoverin differently change their overall hydrophobic properties in response to Ca2+. Using native bovine GCAP1, GCAP2 and recoverin we show that: i) the Ca2+-dependent binding of recoverin to Phenyl-Sepharose is distinct from such interactions of GCAPs; ii) fluorescence intensity of 1-anilinonaphthalene-8-sulfonate (ANS) is markedly higher at high [Ca2+]gfree (10 μM) than at low [Ca2+]free (10 nM) in the presence of recoverin, while an opposing effect is observed in the presence of GCAPs; iii) fluorescence resonance energy transfer from tryptophane residues to ANS is more efficient at high [Ca2+]free in recoverin and at low [Ca2+]free in GCAP2. Such different changes of hydrophobicity evoked by Ca2+ appear to be the precondition for possible mechanisms by which GCAPs and recoverin control the activities of their target enzymes.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 2; 367-376
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    p19 detected in the rat retina and pineal gland is a guanylyl cyclase-activating protein (GCAP).
    Autorzy:
    Dejda, Agnieszka
    Matczak, Izabela
    Gorczyca, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1043693.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    pineal gland
    rat
    guanylyl cyclase
    calcium-binding proteins
    guanylyl cyclase-activating proteins
    retina
    Opis:
    The Ca2+-dependent activation of retina-specific guanylyl cyclase (retGC) is mediated by guanylyl cyclase-activating proteins (GCAPs). Here we report for the first time detection of a 19 kDa protein (p19) with GCAP properties in extracts of rat retina and pineal gland. Both extracts stimulate synthesis of cGMP in rod outer segment (ROS) membranes at low (30 nM) but not at high (1 mM) concentrations of Ca2+. At low Ca2+, immunoaffinity purified p19 activates guanylyl cyclase(s) in bovine ROS and rat retinal membranes. Moreover, p19 is recognized by antibodies against bovine GCAP1 and, similarly to other GCAPs, exhibits a Ca2+-dependent electrophoretic mobility shift.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 4; 899-905
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Particulate guanylyl cyclases: multiple mechanisms of activation.
    Autorzy:
    Kobiałka, Marcin
    Gorczyca, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1044281.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    signal transduction
    calcium-binding proteins
    guanylyl cyclases
    cyclic nucleotides
    Opis:
    Cyclic GMP (cGMP), a key messenger in several signal transduction pathways, is synthesized from GTP by a family of enzymes termed guanylyl cyclases, which are found in two forms: cytosolic (soluble) and membrane-bound (particulate). The past decade has brought significant progress in understanding the molecular mechanisms that underlie the regulation of particulate guanylyl cyclases and new members of their family have been identified. It has become more evident that the basic mechanism of catalysis of guanylyl cyclases is analogous to that recognized in adenylyl cyclases. Here we review the known basic mechanisms that contribute to the regulation of particulate guanylyl cyclases.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 3; 517-528
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-5 z 5

      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