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A precise method has been developed for measuring the activity of Ornithine decarboxylase \(ODC) enzyme, a promising target of cancer and infectious diseases using petite quantity of chemicals.The modi ed spectrophotometric assay has been used to nd inhibitors of ODC enzyme.The methodology is based on the cognizance that enzyme transforms L-ornithine hydrochloride \(substrate) to yellow colored putrescine \(product) soluble in pentanol, the absorbance of which was measured spectrophotometrically.The technique described herein was optimized for evaluating e cacy of phytomolecules as ODC attenuator but could also be used for exploration of novel bioactive compounds as chemopreventive and/or chemotherapeutic agents.A reaction concoction was prepared and hydrophobic withdrawal of yellow colored TNP-Putrescine-TNP complex was recorded at 426nm.Advanced validation and understanding of the factors affecting the enzyme activity i.e. substrate concentration, inhibitor concentration, temperature, pH of the reaction medium and incubation time were also investigated.
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Luqman et al. (2013) studied this question.
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