Abstract
A highly sensitive bioluminescent assay of dehydrogenases was performed. NADH was produced by the catalytic action of alcohol and glucose-6-phosphate dehydrogenases and subsequently measured with high sensitivity by a bioluminescent assay using NAD (P) H : FMN oxidoreductase and luciferase from Photobacterium fischeri. The minimal amount of dehydrogenases that could be measured was 0.0055 amol (5.5 × 10-21 mol).