Xanthine oxidase activity in rat brain

摘要: Abstract Xanthine oxidase activity was demonstrated in rat brain preparations by a spectrofluorometric method using pterine as substrate. The of the enzyme cytosol 10 ± 4.3 nmoles/g protein per h (mean S.D.) compared with an 46.0 24.9 μmoles/g liver cytosol. Column chromatography on Sephadex G-150 dextran resulted elution two peaks 280 nm absorption. first peak contained xanthine 174-fold increase total over that measurable applied to column, and specific 2620.4 h. second inhibitor assay. Similar only 1.54-fold yield activity, slight 54.9 no detection inhibitor. separated from identified hypoxanthine paper its characteristic ultraviolet spectra. had temperature pH optima, apparent molecular weight, kinetic properties similar those enzyme. presence tissue could contribute regulation purine metabolism brain.