Continuous monitoring of reactions that produce NADH and NADPH using immobilized luciferase and oxidoreductases from Beneckea harveyi
✍ Scribed by Colin Haggerty; Edward Jablonski; Laureen Stav; Marlene DeLuca
- Book ID
- 102985584
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 628 KB
- Volume
- 88
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
Highly purified NADH and NADPH:FMN oxidoreductase and luciferase isolated from Beneckea harveyi have been immobilized to arylamine glass beads which were cemented to glass rods. The immobilized enzyme rods are stable, reuseable, and specific for either NADH or NADPH. These rods have been used to monitor reactions producing NADH or NADPH. Picomole levels of malate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase, glucose-6phosphate dehydrogenase, and hexokinase have been assayed using these rods. Glucose determination has been carried out using soluble hexokinase and glucose-6-phosphate dehydrogenase and the immobilized luciferase-oxidoreductase enzymes. Determination of ethanol concentrations as low as 0.0004% has been achieved with an immobilized alcohol dehydrogenase-NADH:FMN oxidoreductase-luciferase rod.