Several plant hormones and analogues were tested for their inhibitory
effects on xanthine oxidase. The flavoprotein enzyme, xanthine oxidase
, catalyses the oxidation of hypoxanthine to xanthine and then xanthin
e to uric acid which has lambda max 295 nm. uric acid was thus the bas
is for a spectrophotometric assay of the activity of xanthine oxidase.
The results showed that trans-zeatin displayed the strongest activity
(IC50=23.5 mu M) on xanthine oxidase inhibition, followed by indole-3
-acrylic acid (IC50=136.0 mu M) and then by the mixed isomers of zeati
n (trans-zeatin and cis-zeatin) (IC50=198.65 mu M). Trans-zeatin induc
ed an uncompetitive inhibition of the enzyme with respect to the subst
rate xanthine and the apparent inhibition constant (Ki) was 5.09 mu M.
However, zeatin riboside was inactive. Since xanthine oxidase serum l
evels are increased in hepatitis, mild hepatic intoxication, tumours b
rain tissues, and DNA damage induced by cytotoxic agents, it is expect
ed that trans-zeatin may be useful for the treatment of these diseases
as well as gout which is caused by deposition of uric acid in the joi
nts and oxidative damage of tissue caused by generation of superoxide
anion radical.