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Pharmaceutics
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IDENTIFICATION OF ALDEHYDE OXIDASE AS AN ENZYME IN METABOLISM OF ZONIPORIDE


Abstract

Author(s): Sagar Shrikantrao Deshmukh*, Amit Suryakant Tapkir, Praveen Chaudhari

Aldehyde oxidases are molybdoflavoenzymes present in cytosolic compartment with broad substrate specificity, oxidizing different types of aldehydes, and heterocyclic rings has attracted increased interest in recent years. The physiological function of aldehyde oxidases is largely unknown, although the enzymes play an important role in the metabolism of numerous compounds of medicinal and toxicological interest, as they oxidize a wide range of aldehydes and heterocyclic compoundsAldehyde oxidase. This unit provides methods for identification and confirmation of AO as metabolic pathways that are AO substrate as well as the effect of different protein (Human S9 fractions) concentration on different concentrations of zoniporide. The peak at3.29 min is Metabolized zoniporide whilethe peak at m/z 337 (RT = 3.22 min) suggests an addition of 16 amu to zoniporide. The maximum formation of metabolite shown up to 90 min in both protein concentrations respectively, further 90 min it decreases rapidly.

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