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  • Book
    Gardner, David G.; Greenspan, Francis S.; Shoback, Dolores M.
    Digital Access
    Provider
    Version
    AccessMedicine
    10th ed. (2018)
    AccessMedicine
    9th ed. (2011)
    Print Access Request
    Location
    Version
    Call Number
    Items
    Books: General Collection (Downstairs)
    2007-<2018>
    RC648 .B312
    3
  • Book
    Contents:
    Sicherheitsbedürfnisse im Bereich gentechnologischer Produktionen / Gerhard Korger
    Ernst Mach (1838-1916) / Ludwig J. Weigert
    Langzeit-Windkanalmessungen liefern Vergleichsdaten für Fragen der Energetik und des Wasserhaushalts von Zugvögeln / Werner Nachtigall
    Zur Chirurgie des Dickdarmkrebses / Franz Karl Mörl
    Vergleichende anatomische Forschung und die Praxiz in der Allgemeinchirurgie / Friedrich Stelzner
    Versunkene Gedanken, oder: Verrat an den beschworenen Gelübden der Gedankenfreiheit / Gerhard Pfohl
    50 Jahre Forschung und Entwicklung auf dem Gebiet Turbostrahlantriebe (1938/39 bis 1988/89) / Hans-Georg Münzberg.
    Print c1989
  • Article
    Harrison LI, Christensen HN, Handlogten ME, Oxender DL, Quay SC.
    J Bacteriol. 1975 Jun;122(3):957-65.
    The uptake of L-4-azaleucine was examined in Escherichia coli K-12 strains to determine the systems that serve for its accumulation. L-4=Azaleucine in radio-labeled form was synthesized and resolved by the action of hog kidney N-acylamino-acid amidohydrolase (EC 3.5.1.B) on the racemic alpha-N-acetyl derivative of DL-[dimethyl-14C]4-azaleucine. L-4-Azaleucine is taken up in E. coli by energy-dependent processes that are sensitive to changes in the pH and to inhibition by leucine and the aromatic amino acids. Although a single set of kinetic parameters was obtained by kinetic experiments, other evidence indicates that transport systems for both the aromatic and the branched-chain amino acids serve for azaleucine. Azaleucine uptake in strain EO317, with a mutation leading to derepression and constitutive expression of branched-chain amino acid (LIV) transport and binding proteins, was not repressed by growth with leucine as it was in parental strain EO300. Lesions in the aromatic amino acid transport system, aroP, also led to changes in the regulation of azaleucine uptake activity when cells were grown on phenylalanine. Experiments on the specificity of azaleucine uptake and exchange experiments with leucine and phenylalanine support the hypothesis that both LIV and aroP systems transport azaleucine. The ability of external azaleucine to exchange rapidly with intracellular leucine may be an important contributor to azaleucine toxicity. We conclude from these and other studies that at least four other process may affect azaleucine sensitivity: the level of branched-chain amino acid biosynthetic enzymes; the level of leucine, isoleucine, and valine transport systems; the level of the aromatic amino acid, aroP, uptake system; and, possibly, the ability of the cell to racemize D and L amino acids. The relative importance of these processes in azaleucine sensitivity under various conditions is not known precisely.
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