The assay of uridine diphosphoglucose dehydrogenase activity: discrimination from xanthine dehydrogenase activity.
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.
Mehdizadeh
S
S
Unit of Cellular Pharmacology and Toxicology, Robens Institute of Health and Safety, University of Surrey, Guildford, U.K.
Bitensky
L
L
Chayen
J
J
D000818:Animals; D002358:Cartilage, Articular / Q000201:enzymology; D004795:Enzyme Stability / Q000187:drug effects; D005260:Female; D007700:Kinetics; D008773:Methylphenazonium Methosulfate / Q000494:pharmacology; D051379:Mice; D008808:Mice, Inbred CBA; D009243:NAD / Q000494:pharmacology; D011190:Potassium Cyanide / Q000494:pharmacology; D014533:Uridine Diphosphate Glucose Dehydrogenase / Q000378:metabolism*; D014968:Xanthine Dehydrogenase / Q000378:metabolism*
D009243:NAD; D008773:Methylphenazonium Methosulfate; D014533:Uridine Diphosphate Glucose Dehydrogenase; D014968:Xanthine Dehydrogenase; D011190:Potassium Cyanide