• Food Science and Preservation
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• v.13 no.5
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• pp.616-622
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• 2006

This study was intended to analyze the contents of polyphenol compounds and vitamin C, and the inhibitory activities of xanthine oxidase and tyrosinase to measure physiological efface of various extract of Lespedeza bicolor. The vitamin C content was $26.42{\pm}0.08mg/100g$. The content of phenolic compounds included in the flesh L bicolor was $1.14{\pm}0.02mg/g$. The ethanol extract by reflux method and water extracts by the microwave-assisted method showed the highest content as 154.95 mg/g and 145.17 mg/g, respectively. The xanthine oxidase inhibitory tate of water extracts was the highest value of 87.85% at the concentration of 1,000 ug/mL. All kinds of extracts showed the highest inhibitory activity for the xanthine oxidase at the concentration of 1,000 ug/mL and a decreasing pattern of the inhibitory race over the concentration of 1,000 ug/mL. The tyrosinase inhibitory rate was increased with an increment of the extract concentrations, and the activity of ethanol extracts was the highest as 55.22% at the concentration of 3,000 ug/mL.

• Journal of Mushroom
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• v.12 no.1
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• pp.1-7
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• 2014

This study was initiated to investigate antioxidant, anti-acetylcholinesterase, and xanthine oxidase inhibitory activities and properties of fruiting bodies, mycelia, and fermentation culture filtrates from Phellinus igniarius. The contents of total phenols and flavonoid of fruit bodies, mycelia, and culture filtrate were 15.35-1.36 mg/g, 10.35-7.85 mg/g, and 8.25-5.36 mg/g. The 1,1-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging abilities of the extracts from the fruiting bodies, mycelia, and culture filtrates were 90.25-95.60%, 78.82-85.24%, and 76.32-82.50% at $50-400{\mu}g/mL$, respectively. The chelating ability of fruiting body extract on ferrous ions was higher than those of mycelia and culture filtrates tested. The anti-acetylcholinesterase inhibitory activity of the fruiting body extract at 400 ${mu}g/mg$ exhibited 91.10% on AChE, which is lower than that of positive control, galanthamine (94.82%). The xanthine oxidase inhibitory activities of the fruiting bodies, mycelia, and culture extract were 85.47%, 78.13%, and 72.49% at 400 ${\mu}g/mL$, respectively. Overall, the fruiting body extract has better anti-acetylcholinesterase, antioxidant and xanthine oxidase inhibitory activities than those from mycelia and culture filtrate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.678-684
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• 1993

To evaluate the role of xanthine oxidase in liver damage by CCl4, a group of rats were fed tungstate for a month, which suppressed the activities of xanthine oxidase in serum and liver. Control group of rats were fed standard diet without tungstate. Liver damage was induced both in tungstate fed and control groups by two intraperitoneal injections of CCl4 at the level of 0.1ml/100g body weight at intervals of 24 hours. Increases in the levels of serum alanine aminotransferase by CCl4 were significantly smaller in tungstate fed rats than in control rats. Concomitantly, histopathologic changes were less in tungstate fed rats than in control ones. In rats either treated with CCl4 or not, hepatic type O xanthine oxidase activities were remarkably reduced by tungstate feeding. Hepatic aniline hydroxylase activities were higher in rats fed tungstate than control rats when animals were not treated with CCl4, but the enzyme activities were lower in tungstate fed rats than control when they were treated with CCl4. Neither tungstate feeding nor CCl4 treatment caused any significant changes in hepatic glutathione contents, and activities of hepatic glutathione S-transferase, glutathione peroxidase and superoxide dismutase. It is concluded xanthine oxidase reaction augment CCl4 induced liver damage via oxygen free radical system.

• Analytical Science and Technology
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• v.36 no.1
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• pp.44-52
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• 2023

This protocol clarifies a simple and precise method for measuring the activity of xanthine oxidase (XO) enzyme inhibitor. XO enzyme, which accelerates oxidative stress-related disorders through its capacity to generate hydrogen peroxide and superoxide anion radicals (O₂^•-), has been found to be inhibited by several plant extracts. Enzyme samples were incubated with a suitable buffer containing adequate amounts of xanthine as a substrate to determine XO activity. The method depends on direct measurements of uric acid and hydrogen peroxide production to test XO with and without interference. The CUPRAC reagent (Cu(Nc)₂²⁺) was used to inhibit enzyme reaction after incubation was complete. The generated urate and peroxide reduced the Cu(II)-neocuproine complex (Cu(Nc)₂²⁺) to a brightly colored Cu(I)-neocuproine complex (Cu(Nc)₂⁺), which was assessed with a spectrophotometer at 450 nm. XO activity was found to be directly related to the increased absorbance of the colored Cu(I)-neocuproine complex (Cu(Nc)₂⁺). To eliminate catalase enzyme interference, the proposed method used sodium azide and was validated against XO activity using the UV method in matched samples with t-test analysis. The proposed assay can determine XO activity with high precision, as indicated by the correlation coefficient (R² = 0.9935) from comparison with the reference protocol.

• Journal of the East Asian Society of Dietary Life
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• v.7 no.1
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• pp.21-27
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• 1997

To evaluate the effect of ethanol pretreatment on the liver and serum xanthine oxidase(XO) activity, the bromobenzene(40mg/kg body wt., i.p.) was orally given 3 times daily to the Sprague-Dawley male rats pretreated with 5% ethanol throughout 2 months. Bromobenzene treated rats pretreated with ethanol showed the more decreased activity of serum and liver XO, and lower value of V than those of only bromobenzene treated rats. Bu the bromobenzene treatment, ethanol pretreated rats showed the more decreased levels of serum alanine aminotransferase activity and liver weight/bo여 weight(%), and decreased degree of liver damage on histopathological observation than the control group.

• Archives of Pharmacal Research
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• v.17 no.5
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• pp.318-322
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• 1994

Upon gel filtration, the commercial bovine milk xanthine oxidase preparation was fractionated into two preparations showing enzyme activity. Native polyacrylamide gel electrophoresis showed that one was in a dimeric form and the other was a monomer having molecular weight of 150 kDa. It was also found that this commercial enzyme existed mostly in an active monomeric form without loss of enzyme activity. The rabbit antisera produced against two enzyme preparations cross-reacted well each other. In SDS-polyacrylamide gtel electro-phoresis, however, both enzyme preparations yielded two smaller protein bands below 150 kDa, which appeared to bind with both antisera with high affinity but not to retain enzyme activity. It implies that bovine milk xanthine oxidase can lose its activity when monomeric subunit is further degraded.

• Archives of Pharmacal Research
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• v.21 no.3
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• pp.236-240
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• 1998

The effect of thyroid hormones on the hepatic xanthine oxidase activity was studied in rats after the intraperitoneal injections of comthyroid (triiodotyronine:thyroxine=1:4) at 0.3 mg/kg for 3 consecutive days. The aim of this study was to understand the precise mechanism of hyperthyroidism induced by oxidative stress. The concentration of lipid peroxides determined indirectly by the measurement of thiobarbituric acid reactants was increased in comthyroid treated rats. The hepatic glutathione content was decreased in comthyroid injected rat compared to the euthyroid state. It was also observed that the increment of xanthine oxidase activity has a profound role in oxygen radicals generation system in comthyroid treated rat. These findings suggest that the enhanced xanthine oxidase activity and depleting glutathione content in comthyroid treated rats result in pathophysiological oxidative stress including an increment of hepatic lipid peroxidation.

• Journal of Ginseng Research
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• v.11 no.1
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• pp.24-31
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• 1987

We studied a assay method on the measurement of superoxide dismutase (SOD Superoxide : superoxide oxidoreductase, EC. 1. 15. 1. 1) activity with photoreduced flavin and nitroblue tetrazolium (NBT) as superoxide (${O_2}^{-}$) source and detector, respectively. The $\Delta$E (1000 ng SOD$.$$min.)^{-1}$ of photoreduced flavin-NBT system was 0.08, whereas that of xanthine-xanthine-cytochrome system used broadly in experiments was 0.014. Therefore, the new method was regarded more simple and utilizable than xanthine-xanthine cytochrome system method. In the present paper, we also carried out to investigate the SOD activity and isozyme pattern for the parpose of study of leaf-burning disease in ginseng (Panax ginseng C.A. Meyer) leaves.

• Journal of Environmental Health Sciences
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• v.16 no.1
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• pp.67-74
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• 1990

An effect of carbon tetrachloride (CCl$_{4}$) was studied on the xanthine oxidase(XOD)activity of small intestine in male rats. Concomitantly a cause of increasing small intestine XOD was focused on an effect of actinomycin D and the kinetics of partial purified XOD frdm small intestine in CCl$_{4}$ intoxicated rats. An injection of CCl$_{4}$ to the rats showed an increase of small intestine XOD. In the pretreatment of actinomycin D before injection of CCl$_{4}$ to the rats, the XOD activities of small intestine were significantly decreased. In the partial purified enzyme preparation, the small intestine XOD in CCl$_{4}$ intoxicated rats showed the more increased Km and Vmax value with xanthine as substrate than that of control group.

• The Journal of Korean Medicine
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• v.17 no.2 s.32
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• pp.191-202
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• 1996

Cervus elaphus for herb-acupuncture solution(CEHAS) was tested for the effects of free radical generating enzyme and lipid peroxidation in rat's liver. In vitro, levels of lipid peroxide in tissues of liver were proportionally decreased to concentration of CEHAS. They were much more decreased. when lipid peroxidation was induced with ferrous iron $(Fe^{-2})$. Also, enzyme activities of xanthine oxidase were decreased. The ratio of type conversion of xanthine oxidase was lowered, too. But, here was not special changes on enzyme activities of aldehyde oxidase. These results suggest that CEHAS decrease the activities of free radical generating enzymes such as xanthine oxidase which form lipid peroxide.