Aldehyde oxidase activity and stability in water-miscible organic solvents.

In this study, the catalytic activity of aldehyde oxidase was investigated in various water-miscible organic solvents for the first time. The enzyme was partially purified from rabbit liver, and its activity was determined in the absence/presence of nine hydro-organic mixtures. The effects of pH and temperature on the enzyme activity were also investigated.

A highly sensitive RP-HPLC-fluorescence method to study aldehyde oxidase activity.

Aldehyde oxidase is a widely distributed enzyme that is involved in the metabolism of an extensive range of aldehydes and N-heterocyclic compounds with physiological, pharmacological, and toxicological relevance. In the present study, a highly sensitive RP-HPLC-fluorescence method based on the oxidation of phenanthridine to phenanthridinone has been developed and validated to assay aldehyde oxidase activity in biological samples. Determination of phenanthridinone was achieved on a C18 column using 10 mmol/L phosphate buffer (pH 5.