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  • 1
    Electronic Resource
    Electronic Resource
    Superoxide dismutase activity of the captopril-iron complex (1995)
    Springer
    Molecular and cellular biochemistry 146 (1995), S. 45-47 
    Details
    ISSN: 1573-4919
    Keywords: captopril ; superoxide anion ; iron ; chelating reagent ; ischemia-reperfusion injury ; free radicals
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract With an assay that generates superoxide anion radicals without the intervention of metal ions we investigated the antioxidant properties of captopril, an angiotensin-converting enzyme inhibitor with a sulfhydryl group. Under these conditions, increasing concentrations of the drug were seen not to scavenge O· 2 − directly. However, a combination of captopril and iron could bring about the breakdown of the superoxide anion; a result that may help to understand the free radical-scavenging properties of captopril.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00926880
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  • 2
    Electronic Resource
    Electronic Resource
    Inhibition of membrane-bound succinate dehydrogenase by disulfiram (1991)
    Springer
    Journal of bioenergetics and biomembranes 23 (1991), S. 335-343 
    Details
    ISSN: 1573-6881
    Keywords: Disulfiram ; antabuse ; heart mitochondria ; submitochondrial particles ; succinate dehydrogenase ; sulfhydryl groups
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of disulfiram on succinate oxidase and succinate dehydrogenase activities of beef heart submitochondrial particles was studied. Results show that disulfiram inhibits both functions. Succinate and malonate suppress the inhibitory action of disulfiram when succinate dehydrogenase is stabilized in an active conformation. Disulfiram is not able to inhibit the enzyme when succinate dehydrogenase is inactivated by oxaloacetate. The inhibitory effect of disulfiram is reverted by the addition of dithiothreitol. From these results, it is proposed that disulfiram inhibits the utilization of succinate by a direct modification of an -SH group located in the catalytically active site of succinate dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762226
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    Paper (German National Licenses)
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