Abstract
A simple spectrophotometric method for estimation of diamine oxidase (DAO) activity was developed, based on a coupled reaction with NADH-dependent alcohol-dehydrogenase. Cystamine, upon DAO action, is transformed into an aminoaldehyde which reacts quickly and quantitatively with NADH in the presence of liver alcohol dehydrogenase: oxidation rates at 340 nm are linear, with protein concentration over the whole range of purification steps of DAO. The high sensitivity, the possibility of continuous monitoring, and the easy performance with commercially available products allows this new method to be considered comparable to the most diffuse standard methods.
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