Abstract
Xanthine oxidase (XO) is a key enzyme which can catalyze xanthine to uric acid causing hyperuricemia in humans. By using the fractionation technique and inhibitory activity assay, an active compound that prevents XO from reacting with xanthine was isolated from wheat leaf. It was identified by the Mass and NMR as 6-aminopurine (adenine). A structure–activity study based on 6-aminopurine was conducted. The inhibition of XO activity by 6-aminopurine (IC 50 = 10.89 ± 0.13 μM) and its analogues was compared with that by allopurinol (IC 50 = 7.82 ± 0.12 μM). Among these analogues, 2-chloro-6(methylamino)purine (IC 50 = 10.19 ± 0.10 μM) and 4-aminopyrazolo[3,4- d] pyrimidine (IC 50 = 30.26 ± 0.23 μM) were found to be potent inhibitors of XO. Kinetics study showed that 2-chloro-6(methylamino)purine is non-competitive, while 4-aminopyrazolo[3,4- d]pyrimidine is competitive against XO.
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