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  • 1970-1974  (12)
  • 1950-1954  (2)
  • 1940-1944  (11)
  • 1
    Electronic Resource
    Electronic Resource
    Enzymic degradation of heme. Oxygenative cleavage requiring cytochrome P-450 (1972)
    s.l. : American Chemical Society
    Biochemistry 11 (1972), S. 1716-1720 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00759a029
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  • 2
    Electronic Resource
    Electronic Resource
    Über die „isolierte Liniengruppe“ in den 4300 Å-Banden im CH- und CD-Spektrum (1941)
    Springer
    Naturwissenschaften 29 (1941), S. 239-239 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01481847
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  • 3
    Electronic Resource
    Electronic Resource
    The mechanism of action of valinomycin on the thylakoid membrane (1971)
    Springer
    The journal of membrane biology 4 (1971), S. 179-192 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Most of the studies devoted to the mechanism by which certain antibiotics increase the ion permeability ofbiological membranes have been carried out on artificialmodel systems. Undoubtedly one of the major reasons for this was that some of the most relevant biological membrane systems are of submicroscopic dimensions and thus inaccessible to the common electrochemical measuring techniques. This holds for the inner membrane systems of chloroplasts, mitochondria, and retinal rods. Since it is not trivial that a mechanism of action found for a model membrane works as well in a biological one with a much higher structural complexity, it seemed worth-while to study the mechanism of action of ionophorous antibiotics on the above-mentioned biological membranes. In this paper, a nonelectrochemical method for measuring both the voltage and the current across the inner chloroplast membrane (or thylakoid membrane) is established in extension of earlier work. This method is used to characterize the mode of action of valinomycin on the thylakoid membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02431970
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  • 4
    Electronic Resource
    Electronic Resource
    Hämoglobinstoffwechsel und Bilirubinbildung (1974)
    Springer
    Journal of molecular medicine 52 (1974), S. 609-616 
    Details
    ISSN: 1432-1440
    Keywords: Haemoglobin degradation ; bilirubin formation ; heme oxygenase ; macrophages ; glucocorticoids ; Hämoglobinstoffwechsel ; Bilirubinbildung ; Hämoxygenase ; Makrophagen ; Glucocorticoide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Unter physiologischen Bedingungen wird das Häm des Hämoglobins zu Bilirubin IXα abgebaut. Die ausgeprägte Lipidlöslichkeit des ungebundenen Bilirubins kann zu einer intracellulären Anhäufung des Pigmentes mit toxischer Zellschädigung führen. Durch Bindung an Albumin und Konjugation mit Glucuronsäure wird eine Wasserlöslichkeit erreicht, die den Zugang des Bilirubins in das Zellinnere verhindert. Drei Viertel des täglich gebildeten Bilirubins (250–350 mg) entstammen dem Abbau gealterter Erythrocyten und ein Viertel dem Stoffwechsel des Myoglobins und der hämenthaltenden Enzyme. Kinetische Untersuchungen mit radioaktiven Isotopen lassen zwei deutlich trennbare Maxima der Bilirubinausscheidung erkennen: Eine frühe Spitze in den ersten Tagen („early-labeled peak“), die aus dem Katabolismus hämenthaltender Enzyme resultiert und eine späte Spitze, die den Abbau der Erythrocyten nach 120 Tagen Lebensdauer reflektiert. Das Häm wird durch die in den Mikrosomen lokalisierte Hämoxygenase zu Biliverdin und dieses durch die im Cytoplasma lösliche Biliverdinreduktase zu Bilirubin abgebaut. Als Organe des normalen Erythrocytenabbaus weisen die Milz, die Leber und das Knochenmark die höchste Hämoxygenaseaktivität auf. In vitro läßt sich der Abbau von Erythrocyten in peritonealen Makrophagen untersuchen. Nach Erythrophagocytose steigt die normalerweise sehr niedrige Hämoxygenaseaktivität steil an, wobei die Höhe der induzierten Enzymaktivität von der Menge der phagocytierten Erythrocyten und von einem ungestörten Glucosestoffwechsel abhängt. Glucocorticoide reduzieren den Glucosestoffwechsel in Makrophagen und bewirken eine Unterdrückung der Hämoxygenase-Induktion bei unbeeinträchtigter Erythrophagocytose. Die Blockierung der Enzyminduktion ist reversibel auf Grund einer steroid-antagonistischen Wirkung von Glucose kombiniert mit Insulin. Es wird die Möglichkeit diskutiert, daß die Senkung des Bilirubinspiegels bei den verschiedenen Formen des hepatogenen Ikterus unter Glucocorticoid-Therapie Ergebnis einer inhibierenden Wirkung des Steroids auf das induzierbare Hämoxygenase-System des retikuloendothelialen Systems ist.
    Notes: Summary Under physiologic conditions the heme moiety of haemoglobin is degraded to bilirubin IXα. The lipid solubility of unbound bilirubin may result in intracellular accumulation of the pigment resulting in potential cell toxicity. Binding of the pigment to albumin or conjugation with glucuronic acid or other sugar moieties renders bilirubin water soluble, which limits its penetration into cells and prevents cell damage. Three quarters of the daily formed bilirubin (250–350 mg) are derived from the catabolism of senescent erythrocytes and approximately one quarter from the turnover of heme-containing enzymes and myoglobin. Kinetic investigations using radioactive isotopes demonstrated two distinctly separate maxima of bilirubin formation: an “early-labeled peak” resulting from catabolism of heme-containing enzymes predominantly in the liver, and a late peak reflecting degradation of senescent erythrocytes at the end of their life span. Heme is converted to bilirubin by microsomal heme oxygenase and is further reduced to bilirubin by soluble biliverdin reductase. Heme oxygenase activity is most active in tissues that normally degrade erythrocytes, such as the spleen, liver, and bone marrow. Degradation of erythrocytes has been investigated in peritoneal macrophages in vitro. After erythrophagocytosis, the initially low heme oxygenase activity rose steeply. The degree of enzyme induction is proportional to the amount of phagocytized erythrocytes and is critically dependent on unimpaired glucose metabolism. Glucocorticoids depress glucose metabolism in macrophages and prevent induction of heme oxygenase without interfering with erythrophagocytosis. Repression of enzyme induction is reversible by the steroid-antagonistic action of glucose combined with insulin. The possibility is considered that in various forms of hepatogenous jaundice, the fall of serum bilirubin after glucocorticoid therapy may be caused by suppression of heme oxygenase activity in the reticuloendothelial system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01468795
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  • 5
    Electronic Resource
    Electronic Resource
    Über eine angebliche Konvergenzgrenze im C2-Spektrum (1942)
    Springer
    Naturwissenschaften 30 (1942), S. 420-420 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01475177
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  • 6
    Electronic Resource
    Electronic Resource
    Homogene Störungen im Bandenspektrum des Silberhydrids (1942)
    Springer
    Naturwissenschaften 30 (1942), S. 751-752 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01488650
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  • 7
    Electronic Resource
    Electronic Resource
    Über das ε-Bandensystem des NO-Moleküls (1943)
    Springer
    Naturwissenschaften 31 (1943), S. 203-203 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01481914
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    Paper (German National Licenses)
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  • 8
    Electronic Resource
    Electronic Resource
    Die Reaktion von Aluminium(III) chlorid mit Triphenylchlormethan in Acetonitril (1971)
    Springer
    Monatshefte für Chemie 102 (1971), S. 806-810 
    Details
    ISSN: 1434-4475
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Auf Grund von Relaxationsmessungen wird unter Berücksichtigung früherer experimenteller Ergebnisse ein Schema der Gleichgewichte von AlCl3 in Acetonitril (AN) angegeben.
    Notes: Abstract The equilibria in solutions of aluminium(III) chloride in acetonitrile are deduced from relaxation measurements and other experimental results.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01167263
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  • 9
    Electronic Resource
    Electronic Resource
    Die Ionisation von Triphenylchlormethan durch Metallchloride in Acetonitril (1971)
    Springer
    Monatshefte für Chemie 102 (1971), S. 798-805 
    Details
    ISSN: 1434-4475
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung In Acetonitril (AN) werden die Bruttogeschwindigkeitskonstanten der Reaktionen $$Ph_3 CCl + MCl_n ANPh_3 C^ + MCl_{n + 1}^ - + AN$$ (MCl n =SbCl5, GaCl3, InCl3 und FeCl3) mit Hilfe des Temperatursprungverfahrens bestimmt. Auf Grund der Relaxations-spektren wird angenommen, daß bei den untersuchten Metall(III)-chloriden in verd. Lösung folgende Gleichgewichte vorliegen: $$\begin{gathered} 2 MCl_3 AN + 6AN \rightleftharpoons [MCl_2 (AN)_4 ]^ + [MCl_4 ]^ - + 4 AN \rightleftharpoons \hfill \\ 2 [MCl_2 (AN)_4 ]^ + Cl - \hfill \\ \end{gathered} $$
    Notes: Abstract In acetonitrile (AN) solutions the gross constants are determined for the reactions $$Ph_3 CCl + MCl_n ANPh_3 C^ + MCl_{n + 1}^ - + AN$$ (MCl n =SbCl5, GaCl3, InCl3, and FeCl3). The relaxation spectra are interpreted for the reactions of metal(III) chlorides according to the equilibria $$\begin{gathered} 2 MCl_3 AN + 6AN \rightleftharpoons [MCl_2 (AN)_4 ]^ + [MCl_4 ]^ - + 4 AN \rightleftharpoons \hfill \\ 2 [MCl_2 (AN)_4 ]^ + Cl - \hfill \\ \end{gathered} $$
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01167262
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  • 10
    Electronic Resource
    Electronic Resource
    Kinetik der Redoxreaktion von Eisen(III) mit Ferrocen in verschiedenenEPD-Lösungsmitteln Kinetische Untersuchungen in nichtwäßrigen systemen mit Hilfe des Temperatursprungverfahrens, 4. Mitt. (1973)
    Springer
    Monatshefte für Chemie 104 (1973), S. 864-875 
    Details
    ISSN: 1434-4475
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Mit Hilfe des Temperatursprung-Relaxationsverfahrens wurde die Kinetik der Reaktion $$\begin{gathered} [Fe^{ + III} (EPD)_6 ](ClO_4 )_3 + Fe^{ + II} (cp)_2 \mathop \rightleftharpoons \limits_{k_2 }^{k_1 } [Fe^{ + II} (EPD)_6 ](ClO_4 )_2 + \hfill \\ + Fe^{ + III} (cp)_2 ClO_4 \hfill \\ \end{gathered} $$ in den Lösungsmitteln Nitromethan (NM), Acetonitril (AN), Trimethylphosphat (TMP), Dimethylformamid (DMF), Diäthylformamid (DÄF), Dimethylacetamid (DMA) und Dimethylsulfoxid (DMSO) untersucht. Für die Reaktion von Fe(III) mit Fe(cp)2 wird in Lösungsmitteln hoherDN ein Inner-Sphere-Mechanismus mit Übertragung von Cyclopentadienid-Ionen angenommen. InDMF, DÄF, DMA undDMSO werden die Geschwindigkeitskonstantenk 1 undk 2 mit steigenderDN desEPD kleiner. Mit steigenderDN desEPD nimmt die Geschwindigkeitskonstante der Reaktion 3 Fe(cp)2ClO4+6EPD→2 Fe(cp)2+[Fe(EPD)6](ClO4)3+2 C5H5 zu.
    Notes: Abstract The kinetics of the reaction $$\begin{gathered} [Fe^{ + III} (EPD)_6 ](ClO_4 )_3 + Fe^{ + II} (cp)_2 \mathop \rightleftharpoons \limits_{k_2 }^{k_1 } [Fe^{ + II} (EPD)_6 ](ClO_4 )_2 + \hfill \\ + Fe^{ + III} (cp)_2 ClO_4 \hfill \\ \end{gathered} $$ has been studied in nitromethane, acetonitrile, trimethyl phosphate, dimethylformamide, diethylformamide, dimethylacetamide and dimethylsulphoxide solution by the temperature-jump technique. For the reaction between Fe(III) and Fe(cp)2 in solvents of highDN an inner-sphere mechanism with transfer of cyclopentadienide groups is suggested. The rate konstantsk 1 andk 2 inDMF, DEF, DMA, andDMSO are given. They decrease with increasingDN. The rate constant of the reaction 3 Fe(cp)2ClO4+6EPD→2 Fe(cp)2+[Fe(EPD)6](ClO4)3+2 C5H5 increases with increasingDN of theEPD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00910598
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