They were kept at room temperature without any stress after the administration of DMSO. The stomach of each animal was processed for MSA, which was allowed to react with the fast blue BB salt to yield a yellow product. This was measured spectrophotometrically at 425 nm using benzenesulfonic acid as standard. Values obtained were expressed as nmol

of °OH generated per g of stomach. XO activity of the rat gastric tissue was assayed by measuring the conversion of xanthine to uric acid [19]. Briefly, the weighed amount of gastric tissue was homogenized in cold (10%) in 50 mM phosphate buffer, pH 7.8. The homogenates were centrifuged check details at 500 g for 10 min. The resulting supernatant was further centrifuged at 12,000 g for 20 min in cold.

The supernatant, thus obtained, was collected and used for spectrophotometric assay of the enzyme at 295 nm using 0.1 mM xanthine in 50 mM phosphate buffer, pH 7.8, as the substrate. The enzyme activity was expressed as milli units/min/mg tissue protein. The activity of XDH was measured by following the reduction of NAD+ to NADH according to the method of [42]. In brief, the weighed amount of rat gastric tissue was homogenized in cold (10%) in 50 mM phosphate buffer with 1 mM EDTA, pH 7.2. The homogenates were centrifuged in cold at 500 g for 10 min. The supernatant, thus obtained, was further centrifuged in cold at 12,000 g for 20 min. The final supernatant was used as the source of the enzyme, and the activity of the enzyme was measured spectrophotometrically at 340 nm with 0.3 mM xanthine Tyrosine Kinase Inhibitor Library high throughput as the substrate (in 50 mM phosphate buffer, pH 7.5) and 0.7 mM NAD+ as an electron donor. The enzyme activity was expressed as milli units/min/mg tissue protein. The weighed amount of rat gastric tissue was homogenized (10%) in ice-cold 50 mM phosphate buffer, pH 7.4 with a Potter Elvenjem glass homogenizer (Belco Glass Inc., Vineland, NJ, USA) for 30 s. The homogenates were then centrifuged at 500 g for 10 min. The supernatant, thus obtained, was again centrifuged at 12,000 g Carnitine dehydrogenase for 15 min to obtain a

pellet containing mitochondria. This pellet was again suspended in the buffer and used for measuring the activities of the mitochondrial enzymes. The PDH activity was measured spectrophotometrically [14] with some modifications by following the reduction of NAD+ to NADH at 340 nm using 50 mM phosphate buffer, pH 7.4, 0.5 mM sodium pyruvate as the substrate and 0.5 mM NAD+ in addition to the enzyme. The enzyme activity was expressed as units/min/mg tissue protein. Isocitrate dehydrogenase (ICDH) activity was determined by measuring the reduction of NAD+ to NADH at 340 nm with the help of a UV–VIS spectrophotometer [16]. One ml assay volume contained 50 mM phosphate buffer, pH 7.4, 0.5 mM isocitrate, 0.1 mM MnSO4, 0.1 mM NAD+ and the suitable amount of enzyme.