Literature DB >> 196536

Enzymatic oxidation of diethyldithiocarbamate by xanthine oxidase and its colorimetric assay.

R Fried.   

Abstract

Diethyldithiocarbamate is oxidized in vitro by purified cream xanthine oxidase in the presence of nitro blue tetrazolium and phenazine methosulfate. Disulfiram is formed during the enzymatic or nonenzymatic oxidation. When diethyldithiocarbamate is mixed nonenzymatically with nitro blue tetrazolium, the dye is rapidly reduced, but only in the presence of certain organic solvents. This reaction can be used as a convenient colorimetric assay for diethyldithiocarbamate, which gives a stable color over a wide concentration range.

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Year:  1976        PMID: 196536     DOI: 10.1111/j.1749-6632.1976.tb52884.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  3 in total

1.  Mechanism of inactivation of sheep liver cytoplasmic aldehyde dehydrogenase by disulfiram.

Authors:  T M Kitson
Journal:  Biochem J       Date:  1983-08-01       Impact factor: 3.857

2.  The inactivation of aldehyde dehydrogenase by disulfiram in the presence of glutathione.

Authors:  T M Kitson
Journal:  Biochem J       Date:  1981-10-01       Impact factor: 3.857

3.  Studies on the interaction between disulfiram and sheep liver cytoplasmic aldehyde dehydrogenase.

Authors:  T M Kitson
Journal:  Biochem J       Date:  1978-10-01       Impact factor: 3.857

  3 in total

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