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The assay of uridine diphosphoglucose dehydrogenase activity: Discrimination from xanthine dehydrogenase activity
Author(s) -
Mehdizadeh S.,
Bitensky Lucille,
Chayen J.
Publication year - 1991
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290090207
Subject(s) - dehydrogenase , biochemistry , nad+ kinase , chemistry , substrate (aquarium) , cofactor , xanthine dehydrogenase , enzyme , biology , xanthine oxidase , ecology
The biochemical and quantitative cytochemical assays of the activity of uridine diphosphoglucose dehydrogenase (UDPG‐D) have produced perplexing results. It is now shown that the perplexity may be due to the possibility that the coenzyme (NAD) required for UDPG‐D activity, may be acting as a substrate for a second dehydrogenase, namely xanthine dehydrogenase, which may utilize NAD as its substrate. The activity of UDPG‐D can be distinguished selectively by the pH of its optimal activity and by decreasing the concentration of the coenzyme used in the assay.