| Literature DB >> 1934310 |
S Mehdizadeh1, L Bitensky, J Chayen.
Abstract
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.Entities:
Mesh:
Substances:
Year: 1991 PMID: 1934310 DOI: 10.1002/cbf.290090207
Source DB: PubMed Journal: Cell Biochem Funct ISSN: 0263-6484 Impact factor: 3.685