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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Cellular and molecular life sciences 45 (1989), S. 1066-1070 
    ISSN: 1420-9071
    Schlagwort(e): Acrylamide ; nitrile hydratase ; P. chlororaphis B23
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary In this paper an explanation is given of howPseudomonas (P.) chlororaphis B23 can accumulate so much acrylamide of such high purity. One reason is thatP. chlororaphis B23 exhibits much greater nitrile hydratase activity than amidase activity; the rate of formation of acrylamide through the nitrile hydratase reaction is at least 4000 times higher than its breakdown catalyzed by amidase. Furthermore, acrylonitrile, a powerful nucleophilic reagent, inactivates the active thiol residue of the amidase, whereas nitrile hydratase is not so susceptible to acrylonitrile. Thus acrylamide is produced but not transformed further. In addition, the nitrile hydratase purified fromP. chlororaphis B23 exhibits high resistance to a high concentration of acrylamide. Some other explanations, and the results of evaluation of theP. chlororaphis B23 enzyme as a catalyst for the production of acrylamide are discussed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1437-7799
    Schlagwort(e): Key words SMP30 ; Calcium efflux ; Tubular epithelia ; Calcium pump ; Calmodulin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Background. Senescence marker protein-30 (SMP30), a calcium binding protein, is preferentially expressed in the renal proximal tubules and hepatocytes and is presumed to play a role in Ca2+ homeostasis. Methods. To explore its physiological functions in the tubular cells, we investigated the effect of SMP30 on Ca2+ efflux via the ATP-dependent plasma membrane calcium pump. LLC-PK1 cells were stably transfected with a cDNA encoding SMP30, and the established transfectants were subjected to ATP responses. Results. Overexpression of SMP30 significantly increased Ca2+ efflux under both basal and ATP-stimulated conditions. Inhibition of calmodulin by trifluoperazine abrogated the enhanced Ca2+ efflux, suggesting that SMP30 activated the calmodulin-dependent Ca2+ pump. It is known that Ca2+ superfluous influx induces cellular injury. Compared with mock-transfected cells, LLC-PK1 cells expressing SMP30 showed resistance to cellular death triggered by Ca2+ superfluous influx. Conclusion. These results suggest the possibility that, in renal tubular cells, endogenous SMP30 participates in Ca2+ efflux via activating the calmodulin-dependent Ca2+ pump and thereby confers resistance of the cells against injury caused by high intracellular Ca2+ concentrations.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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