Proline Dehydrogenase (ProDH) is a key enzyme that catalyzes proline degradation in mitochondria.
Reducing ProDH activity is very important for regulating osmotic balance, preventing osmotic stress from
damaging plants, scavenging free radicals and protecting cell structure.
ProDH catalyzes the dehydrogenation of proline to pyruvic acid. The dehydrogenation is transferred to
reduce 2,6-dichlorophenol indophenol (DCPIP) by phenazine dimethyl sulfate (PMS), and it has a
characteristic absorption peak at 600 nm. The reduction rate of 2,6-DCPIP is determined by the decrease of
600 nm absorbance, which represents ProDH activity.
Reagents and Equipment Required but Not Provided:
Scales, low temperature centrifuge, spectrophotometer/microplate reader, micro glass cuvette/96 well flat-
bottom plate, acetone, homogenizer/mortar.