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  • 1
    Electronic Resource
    Electronic Resource
    Interaction of Eu3+ with Yeast Alcohol Dehydrogenase (1999)
    Springer
    The protein journal 18 (1999), S. 97-101 
    Details
    ISSN: 1573-4943
    Keywords: Alcohol dehydrogenase ; interaction ; europium ; activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The activity of yeast alcohol dehydrogenase is markedly enhanced by Eu3+ ions. At pH 7.0 two binding constants for Eu3+, 1.0 × 10−2 and 2.0 × 10−3 μM, were obtained using a Scatchard plot. The presence of Zn2+ ions restricts the Eu3+-induced increase in the activity of yeast alcohol dehydrogenase. Studies on the tryptophan fluorescence of the enzyme in the absence and presence of Eu3+ or Zn2+ ions showed that Eu3+ affects tertiary or quaternary structures, which is consistent with its activation of the enzyme. The presence of Zn2+ reverses the conformational changes caused by Eu3+. Comparison of the effects of Eu3+ with Zn2+ for apo-yeast alcohol dehydrogenase indicates that their binding sites on the protein are different.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020607818690
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Kinetics of Thermal Inactivation of Lactate Dehydrogenase from Rabbit Muscle (1997)
    Springer
    The protein journal 16 (1997), S. 801-807 
    Details
    ISSN: 1573-4943
    Keywords: Lactate dehydrogenase ; NADH ; nicotinamide adenine dinucleotide, reduced form
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The kinetics of thermal inactivation of rabbit muscle lactate dehydrogenase at different temperatures has been studied using the kinetic method for the substrate reaction during irreversible inhibition of enzyme activity previously described by Tsou [Adv. Enzymol. Relat. Areas Mol. Biol. (1988), 61, 381–436]. The results show that thermal inactivation of the enzyme is an irreversible reaction. Microscopic rate constants were determined for thermal inactivation of the free enzyme and the enzyme–substrate complex. The inactivation rate constant of the free enzyme is much larger than the rate constant of the enzyme–substrate complex. The results suggest that the presence of the substrate has a certain protective effect against thermal inactivation of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026320001709
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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