Activity determination of 3-iodopyridineadenine dinucleotide and its phosphate as hydride acceptors in the presence of dehydrogenases using a coupled redox system.
European journal of biochemistry
confidence
Key findings
Activity measurement method for NAD(P)+-dependent dehydrogenases; 3-iodopyridineadenine dinucleotide active with alcohol and lactate dehydrogenase but not with glyceraldehyde-3-phosphate or 3-phosphogluconate dehydrogenase.
View source on PubMed (PMID 7007042) ↗
- Sample size
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- Population
- In vitro enzyme assays
- Dosing
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- Duration
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- Blinding
- not_reported
- Controls
- none
- Drug class
- coenzyme
Full abstract
A new procedure for the activity measurement of NAD(P)+-dependent dehydrogenases has been devised using an electron-transferring agent, phenazine methosulfate, and an electron acceptor, 3-(4,5-dimethylthiazolyl)-2,5-diphenyltetrazolium bromide. The reduction of the latter is determined by an increase in absorbance at 578 nm. 3-Iodopyridineadenine dinucleotide was found to be active as an hydride acceptor with horse liver alcohol dehydrogenase and lactate dehydrogenase but showed no activity with glyceraldehyde-3-phosphate dehydrogenase nor did its phosphate with 3-phosphogluconate dehydrogenase.