Aldehyde dehydrogenase (ALDH) has been used to evaluate the effects of pear extracts on ALDH activity. It has also been used to colorimetrically determine ethanol by monitoring the enzymatic reduction of nicotinamide adenine dinucleotide (NAD).
Aldehyde Dehydrogenase, potassium-activated from yeast has been used:
- for enzyme immobilization and to oxidize formaldehyde to formate
- to study the functional relation betweenhydrazone
- to measure ethanol production.
Aldehyde dehydrogenase from baker′s yeast has been used to measure the activity of aldehyde dehydrogenase by Tottmar′s method to determine the change in nicotinamide adenine dinucleotide (NADH) levels in serum sample. It has also been used in pyruvate decarboxylase assay.
Aldehyde dehydrogenase (ALDH) is a soluble enzyme and its activity depends on potassium ions and cysteine. The family of ALDH comprises of 19 genes in human. ALDH gene is expressed in the nucleus, cytosol, mitochondria and endoplasmic reticulum of the cell. ALDH is a component of nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide phosphate (NADPH) recycling systems.
Aldehyde dehydrogenase (ALDH) regulates the non-P450 aldehyde reduction enzyme system. It protects the cell from the effects of toxic aldehydes. Mutations in this gene are associated with Sjogren Larsson syndrome, Larsson syndrome, type II hyperprolinemia and cancer. ALDH takes part in the oxidation of aldehydes to acids. ALDH-2 lowers cardiac ischemia, which arises due to myocardial infarction or post cardiac surgery.
