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  • Inorganic Chemistry  (12)
  • Smooth muscle  (4)
  • Ca current  (2)
  • Ca^2^+ channel  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    FEBS Letters 170 (1984), S. 383-386 
    ISSN: 0014-5793
    Schlagwort(e): Calmodulin ; Contraction control ; Myosin light chain kinase ; Smooth muscle ; Taenia coli
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 0014-5793
    Schlagwort(e): Ca^2^+ channel ; Membrane protein ; Skeletal muscle ; cDNA cloning
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 0014-5793
    Schlagwort(e): Ca^2^+ channel ; Expression ; Primary structure ; Smooth muscle
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    FEBS Letters 251 (1989), S. 191-196 
    ISSN: 0014-5793
    Schlagwort(e): Protein kinase, cyclic GMP-dependent ; Smooth muscle ; cDNA cloning
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    Springer
    Pflügers Archiv 405 (1985), S. 285-293 
    ISSN: 1432-2013
    Schlagwort(e): Cardiac myocytes ; Ca current ; Isoprenaline ; Cyclic AMP ; cAMP-Dependent protein kinase ; Protein phosphorylation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Dose-response relations for the increase in the amplitude of Ca current (I Ca) on external application of isoprenaline (ISP) and internally applied cyclic AMP (cAMP) or catalytic subunit of cAMP-dependent protein kinase (C subunit) were established in single ventricular cells of the guinea pig. An intracellular dialysis technique was used. The threshold concentration was for ISP 10−9 M, for cAMP 3 μM (pipette concentration to which 10−5 M 3-isobutyl-1-methylxanthine was added) and for C subunit around 0.4 μM (pipette concentration). The concentrations for the half-maximal effect were 3.7×10−8 M (ISP), 5.0 μM (cAMP) and 0.95 μM (C subunit) and for the maximum effect 10−6 M (ISP), 15–20 μM (cAMP) and 3–4 μM (C subunit). For all three agents the maximum increase in the Ca current density was similar (a factor of 3–4), suggesting that they converge on the same site of the Ca channel. Accordingly, the effects of cAMP and C subunit onI Ca were non-additive to those of ISP. From these data the relationship both between concentrations of ISP and cAMP and between those of cAMP and active C subunit in terms of their effects onI Ca could be estimated and were compared with those obtained in broken cell preparations. A competitive inhibitor of phosphorylation, 5′-adenylyl-imidodiphosphate (5 mM), greatly reduced the effects of ISP and C subunit onI Ca. Cell dialysis with 3 mM adenosine-5′-(γ-thio)-triphosphate, which produces a dephosphorylationresistant phosphorylation, markedly potentiated the effects of ISP and cAMP onI Ca. The results support the hypothesis that phosphorylation of a protein within, or close to, the Ca channel by cAMP-dependent protein kinase is the mechanism of β-adrenergic stimulation.
    Materialart: Digitale Medien
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  • 6
    Digitale Medien
    Digitale Medien
    Springer
    Pflügers Archiv 407 (1986), S. 123-128 
    ISSN: 1432-2013
    Schlagwort(e): Guinea pig heart ; Ca current ; Phosphorylation cycle
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract The calcium current (I Ca) in the heart is increased by phosphorylation of a protein which is part of, or close to, the Ca channel. The phosphorylation is catalysed by cAMP-dependent protein kinase (cAMP-PK). The question whether dephosphorylated channels are available to open on depolarization was examined in ventricular myocytes of guinea pig by recording whole cellI Ca during dialysis with either regulatory (R) subunit of cAMP-PK or protein kinase inhibitor (PKI) or adenosine-5′-(γ-thio)-triphosphate (ATPγS). The following results were obtained: 1) R subunit reduced and PKI reversed the isoprenaline (ISP)-induced enhancement ofI Ca, suggesting their ability to inhibit cAMP-PK. 2) R subunit and PKI, however, reduced basal (i.e. non β-adrenergically stimulated)I Ca only by about 20%. 3) Dialysis with ATPγS resulted in a slow increase in basalI Ca, presumably due to dephosphorylation-resistant thiophosphorylation. 4) When, however, the cell was dialyzed with PKI the effect of ATPγS was almost completely suppressed, suggesting no detectable phosphorylation related to the channel activity in this condition. These results support the view that even in the dephosphorylated state Ca channels are available to open on depolarization and that phosphorylation by cAMP-PK increases the opening probability.
    Materialart: Digitale Medien
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  • 7
    ISSN: 1432-2013
    Schlagwort(e): Skinned coronary arteries ; Smooth muscle ; Regulation of contractile tone ; cAMP-dependent protein kinase ; cAMP-dependent modulation of contractile tone ; Calmodulin ; Calcium
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Maximally contracted detergent skinned coronary smooth muscle fibres are relaxed by lowering the concentration of free Ca2+. The extent and rate of relaxation depends on the concentration of free Ca2+ and calmodulin (CaM) suggesting that it is the Ca2+. CaM complex which is responsible for maintaining tension. At a fixed concentration of Ca2+ and CaM further relaxation can be achieved by addition of the catalytic subunit of the cAMP-dependent protein kinase (cAMP-kinase). The extent as well as the relaxation rate depend on the concentration of cAMP-kinase (0.01–0.5 μM) and both are antagonized by high concentrations of Ca2+ and CaM. The Ca2+-requirement for obtaining half maximal concentration is shifted from 1.1 μM to 6.3 μM Ca2+ in the presence of 0.5 μM cAMP-kinase. These data indicate that the response of the contractile apparatus to a change in the free [Ca2+] can be modulated by cAMP-kinase at the level of the contractile proteins. It is further suggested that the tone of coronary smooth muscle is determined by the relative and not by the absolute concentrations of Ca2+, CaM and cAMP-kinase.
    Materialart: Digitale Medien
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  • 8
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 534 (1986), S. 7-12 
    ISSN: 0044-2313
    Schlagwort(e): Chemistry ; Inorganic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Beschreibung / Inhaltsverzeichnis: Preparation and Structure of N,N′-DithioformylanilineN,N′-dithioformylaniline was prepared by treating N,N′-dichlormethylaniline [1] with silicon disulfide [2]. The compound is characterized by the results of a X-ray structural analysis (RW = 0.030) as well as its nmr and vibration spectra. N,N′-dithioformylaniline crystallizes in the orthorhombic space group P21212 with a = 537.0(2); b = 745.7(3); c = 1111.5(4) pm; V = 445.1(3) · 106 pm3. The molecule consists of two planar parts; the angle between the plane of the aromatic ring and the plane of the N,N′-dithioformylamino group was determined to 87.7°.
    Notizen: N,N′-Dithioformylanilin konnte durch Umsetzung von N,N′-Dichlormethylanilin [1] mit Siliciumdisulfid [2] dargestellt werden. Die Verbindung ist durch die Ergebnisse einer Röntgenstrukturanalyse (RW = 0,030) sowie ihre NMR- und Schwingungsspektren charakterisiert. N,N′-Dithioformylanilin kristallisiert orthorhombisch in der Raumgruppe P21212 mit Z = 2 und a = 537,0(2); b = 745,7(3); c = 1111,5(4) pm; V = 445,1(3) · 106 pm3. Das Molekül weist zwei planare Bauteile auf; der Winkel zwischen der Ebene des Aromaten und der durch die N,N′-Dithioformylaminogruppe gelegten Ebene wurde zu 87,7° bestimmt.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 9
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 534 (1986), S. 13-18 
    ISSN: 0044-2313
    Schlagwort(e): Chemistry ; Inorganic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Beschreibung / Inhaltsverzeichnis: Crystal and Molecular Structure of N,N′-DiformylanilineN,N′-diformylaniline crystallizes in the monoclinic space group P21/n with Z = 8 and a = 856.1(2), b = 1277.6(3), c = 1306.1(3) pm, β 92.29(2)°, V = 1427.4(5) · 106 pm3. As shown by X-ray structure determination (2642 symmetry independent reflections, RW = 0.034) the molecule exists in two enantiomeric forms. The molecular structure can be described by two planes; the angle between the plane of the aromatic ring and the plane of the N,N′-diformylamino group is 70.1 resp. 108.3°. The results are compared with those obtained for other derivats.
    Notizen: N,N′-Diformylanilin kristallisiert monoklin in der Raumgruppe P21/n mit Z = 8 und a = 856,1(2); b = 1277,6(3); c = 1306,1(3) pm; β = 92,29(2)°; V = 1427,4(5) · 106 pm3. Nach den Ergebnissen der Röntgenstrukturanalyse (2642 symmetrieunabhängige Reflexe; RW = 0,034) existiert das Molekül in zwei enatiomeren Formen. Die Molekülstruktur kann durch zwei Ebenen beschrieben werden; der Winkel zwischen der Ebene des Aromaten und der durch die N,N′-Diformylaminogruppe gelegten Ebene beträgt 70,1 bzw. 108,3°. Die Ergebnisse werden mit denen anderer Derivate verglichen.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
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  • 10
    ISSN: 0044-2313
    Schlagwort(e): Chemistry ; Inorganic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Beschreibung / Inhaltsverzeichnis: Studies on Oxide Catalysts. XXV. Catalytic Activity and Aging Properties of Modified Mordenites in the Cracking of n-OctaneMeH-mordenites (Me = Li, K, Mg, Ca, Ba) were prepared by ion exchange starting with H-mordenite (SiO2/Al2O3 mole ratio = 14). To characterize these samples the cracking of n-octane was used as catalytic test reaction. Surface OH groups and the adsorption of NH3 on these samples were investigated by i. r. spectroscopy. Unaffected by the kind of the exchanged cation the Brönsted acidity of the H-mordenite decreases monotonously with increasing content of the incorporated cation. The catalytic activity and (to a much higher degree) the rate of deactivation by coking during the reaction decrease as the Brönsted acidity decreases. The strong dependence of the Brönsted acidity on the deactivation rate points to a multi-site mechanism of the coking process.
    Notizen: MeH-Mordenite (Me = Li, K, Mg, Ca, Ba) wurden ausgehend von einem H-Mordenit (Molverhältnis SiO2/Al2O3 = 14) durch Ionenaustausch hergestellt. Als Testreaktion zur Katalytischen Charakterisierung diente die n-Octanspaltung. IR-spektroskopisch wurden die OH-Oberflächengruppen und die Adsorption von NH3 an den Proben untersucht. Unabhängig von der Art des eingetauschten Kations sinkt die Brönsted-Acidität des H-Mordenits monoton mit steigendem Gehalt an den eingetauschten Kationen. Die katalytische Aktivität und (im weit Stärkeren Maße) die Desaktivierungsgeschwindigkeit (infolge „Verkokens“ während der Reaktion) sinken symbat mit der Brönsted-Acidität. Die starke Abhängigkeit der Geschwindigkeit der Desaktivierung von der Brönsted-Acidität weist auf einen Mehrzentrenmechanismus für die Verkokung hin.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
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