931 resultados para 5-36
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Welsch (Projektbearbeiter): Aufruf von 14 Urwählern des Berliner 71. Bezirks, nur solche Wahlmänner zu wählen, die den Staatsstreich des 9. November 1848 (Verlegung der Nationalversammlung nach Brandenburg) wieder rückgängig machen und eine Verfassung schaffen, welche im Unterschied zu der vom 5. Dezember 1848 kein Gnadengeschenk darstellt
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Welsch (Projektbearbeiter): Ankündigung, die unerlaubte Entfernung von der Truppe mit Ehren- statt bisher Geldstrafen zu ahnden (öffentliche Anprangerung auf Plakaten)
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The cardiac voltage-gated Na(+) channel, Na(V)1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the electrical impulse in the myocardium. Even subtle alterations of Na(V)1.5 function, as caused by mutations in its gene SCN5A, may lead to many different arrhythmic phenotypes in carrier patients. In addition, acquired malfunctions of Na(V)1.5 that are secondary to cardiac disorders such as heart failure and cardiomyopathies, may also play significant roles in arrhythmogenesis. While it is clear that the regulation of Na(V)1.5 protein expression and function tightly depends on genetic mechanisms, recent studies have demonstrated that Na(V)1.5 is the target of various post-translational modifications that are pivotal not only in physiological conditions, but also in disease. In this review, we examine the recent literature demonstrating glycosylation, phosphorylation by Protein Kinases A and C, Ca(2+)/Calmodulin-dependent protein Kinase II, Phosphatidylinositol 3-Kinase, Serum- and Glucocorticoid-inducible Kinases, Fyn and Adenosine Monophosphate-activated Protein Kinase, methylation, acetylation, redox modifications, and ubiquitylation of Na(V)1.5. Modern and sensitive mass spectrometry approaches, applied directly to channel proteins that were purified from native cardiac tissues, have enabled the determination of the precise location of post-translational modification sites, thus providing essential information for understanding the mechanistic details of these regulations. The current challenge is first, to understand the roles of these modifications on the expression and the function of Na(V)1.5, and second, to further identify other chemical modifications. It is postulated that the diversity of phenotypes observed with Na(V)1.5-dependent disorders may partially arise from the complex post-translational modifications of channel protein components.
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In intact chloroplasts isolated from mature pea leaves (Pisum sativum L.), the large subunit (LSU) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39) was rapidly fragmented into several products upon illumination in the presence of 1 mM dithiothreitol (DTT). Very similar effects on LSU stability could be observed when illuminated chloroplasts were poisoned with cyanide which, like DTT, inhibits important plastid antioxidant enzymes, or when a light-dependent hydroxyl radical-producing system was added to the incubation medium. Moreover, DTT-stimulated light degradation of LSU was markedly delayed in the presence of scavengers of active oxygen species (AOS). It is therefore suggested that light degradation of LSU in the presence of DTT is mainly due to inhibition of the chloroplast antioxidant defense system and the subsequent accumulation of AOS in intact organelles. When chloroplasts were isolated from nonsenescent or senescent leaves, LSU remained very stable upon incubation without DTT, indicating that the antioxidant system was still functional in the isolated chloroplasts during leaf ageing. Our data support the notion that AOS might be important for the degradation of Rubisco in vivo under oxidative stress.
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Vorbesitzer: Bartholomaeusstift Frankfurt am Main
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Trägerband: "Hauptschießen mit dem Stahlbogen... 1573 u. 1578"; Vorbesitzer: Stadtarchiv Frankfurt am Main
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Vorbesitzer: Jakob Heller; Dominikanerkloster Frankfurt am Main
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Trägerband: Inc. oct. 407; Vorbesitzer: Dominikanerkloster Worms; Dominikanerkloster Frankfurt am Main
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Signatur des Originals: S 36/F02545
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Signatur des Originals: S 36/F03762
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Signatur des Originals: S 36/F03763
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Signatur des Originals: S 36/F03764
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Signatur des Originals: S 36/F03767
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Signatur des Originals: S 36/F07018
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Signatur des Originals: S 36/F07406