Inhibitory Effect of Xanthine Oxidase from Tamus communis Roots Extracts/Fraction

  • Fatima ZERARGUI Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria
  • Karima SAFFIDINE Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria
  • Thoraya GUEMMAZ Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria
  • Abderrahmane BAGHIANI Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Abstract

In the course of our phytochemical studies of plant Tamus communis L., methanol soluble extract (EMeOH) (138 g) was chromatographed on a silica gel column. The column was eluted with chloroform and then with chloroform /methanol mixtures of increasing polarity. A total of 52 fractions (400 ml each) were collected and grouped according to their TLC behaviour into 6 main fractions (I-VI).  Total phenolic and flavonoid contents in these extracts were determined by a colorimetric method. Values varied between 73.143±0.009 and 29.214±0.003 equivalent Gallic acid/g lyophilisate. All the extracts showed inhibitory properties on xanthine oxidase, the IC50 ranges from 0.029±0.017 mg/ml to 0.237±0.026 mg/ml. The extracts exhibited an additional superoxide scavenging capacity by using both enzymatic methods and IC50 values ​​range from 0.039±0.023 mg/ml to 0.141±0.086 mg/ml. These results show that Tamus communis L. extracts have strong anti-oxidant effects and may have some clinical benefits.


Keywords: Xanthine oxidase, Antioxidant, Superoxide scavenger, Tamus communis L.

Keywords: Xanthine oxidase, Antioxidant, Superoxide scavenger, Tamus communis L., Xanthine oxidase, Antioxidant, Superoxide scavenger, Tamus communis L.

Downloads

Download data is not yet available.

Author Biographies

Fatima ZERARGUI, Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Karima SAFFIDINE, Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Thoraya GUEMMAZ, Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Abderrahmane BAGHIANI, Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

Laboratory of Applied Biochemistry, Faculty of Nature and Life Sciences. Ferhat Abbas University Setif-1, 19000 Setif, Algeria

References

1. Droge W. Free Radicals in the Physiological Control of Cell Function. PhysiolRev. 2002; 82(1):47-95.
2. Wenxin T, Lili T, Xiyan Y, Jiafu T, Fenglin D, Juan H, Kai G, Keith L, Xianlong Z, The calcium sensor GhCaM7 promotes cotton fiber elongation by modulating reactive oxygen species. 2014.
3. Harrison R. Physiological roles of xanthine oxidoreductase. Drug Metab Rev. 2004; 36:363–375.
4. Emmerson BT. The management of gout. N. Engl. J. Med. 1996; 334:445-451.
5. Wallach S L. The side effects of allopurinol. Hosp. Pract. 33: 22. (ROS) production. New phytol. 1998; 202(2):509–520.
6. Bouloc A, Reygagne P, Lecoz P, Dubertret L, Perforating foot ulceration with allopurinol therapy. Clin. Exp. Dermatol. 1996; 21:351-352.
7. Yale S.H, Yale ES, Mann DS. Fever, rash, and angioedema after a course of allopurinol. Hosp. Pract. 1996; 31:92–94.
8. Benzie IFF. Evolution of dietary antioxidants. Comp. Biochem. Physiol. 2003; 136:113–126.
9. Mclarty JW. ‘Antioxidants and cancer: the epidemiologic evidence’ in Antioxidants and Disease Prevention, H. S. Garewal, Ed., 45–66, CRC Press, New York, NY, USA. 1997.
10. Yang CS, Landau JM, Huang MT, Newmark HL. Inhibition of carcinogenesis by dietary polyphenolic compounds. Annu. Rev. Nutr. 2001; 21:381–406.
11. Demmig-Adams B, Adams WW. Antioxidants in photosynthesis and human nutrition. Science. 2002; 298:2149–2153.
12. Zerargui F, Boumerfeg S, Charef N, Baghiani N, Djarmouni M, Khennouf S, Arrar L, Abu Zarga MH, Mubarak MS, Antioxidant Potentials and Xanthine Oxidase Inhibitory Effect of Two Furanocoumarins Isolated from Tamus communis L. Med. Chem. 2015; 11:506-513.
13. Wong SP, Leong LP, William Koh JH. Antioxidant activities of aqueous extracts of selected plants. Food Chem. 2006; 99:775-783.
14. Bahorun T, Gressier B, Trotin F, Brunet C, Din T, Vasseur J, Gazin JC, Pinkas M, Luyckx M, Gazin M. Oxygen species scavenging activity of phenolic extract from howthorn fresh plant organs and pharmaceutical preparation. Arzneimittelforschung/Drug Res. 1996 ; 46(11):1086 – 1089.
15. Baghiani A, Harrison R, Benboubetra M. Purification and partial characterisation of camel milk xanthine oxidoreductase. Arch. Physiol. Biochem. 2003; 111:407-414.
16. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227:680-685.
17. Avis P G, Bergel F, Bray RC, James DWF, Shooter KV. Cellular constituent, the chemistry of xanthine oxidase. Part II. The homogeneity of crystalline metalloflavoproteine fraction. J. Chem. Soc., 1956; 1212-1219.
18. Robak J, Gryglewski RJ. Flavonoids are scavengers of superoxide anions. Biochem. Pharmacol. 1988; 37:837-841.
19. Bray RC. Molybdenum iron-sulfer flavin hydroxylase and related enzymes. In: “The enzymes” 3ème Ed. PD Boyer Ed. Academic Press, New York. 1975; 12:299-419.
20. McCord, J. M. and Fridovich, I. The reduction of cytochrome C by milk xanthine Oxidase. J. Biol. Chem. 1968; 243:5753-5760
21. Matsumura F, Yamaguchi Y, Goto M, Ichiguchi O, Akizuki E, Matsuda T, Okabe K, Liang J, Ohshiro H, Iwamoto T, Yamada S, Mori K, Ogawa M. Xanthine oxidase inhibition attenuates kupffer cell production of neutrophil chemoattractant following ischemia– reperfusion in rat liver. Hepatology, 1998; 28:1578.
22. Hearse D J, Manning AS, Downey JM, Yellon D M. Xanthine oxidase: A critical mediator of myocardial injury during ischemia and reperfusion? Acta Physiol. Scand. 1986; 548:65-78.
23. Benavente-Garcia O, Castillo J, Marin FR, Ortuno A, Del Rio JA. Uses and properties of Citrus flavonoids. J. Agric. Food Chem. 1997; 45:4505–4515.
24. Cos P, Ying L, Calomme M, Hu JP, Cimanga K, Van Poel B, Pieters L, Vlietink AJ, Vanden Berghe D. structur - activity relationship and classification of Flavonoids as Inhibitors of Xanthine Oxidase and Superoxid scavengers. J. Nat. Prod. 1998; 61:71-76.
25. Boumerfeg S, Baghiani A, Messaoudi D, Khennouf S, Arrar L. Antioxidant Properties and Xanthine Oxidase Inhibitory Effects of Tamus communis L. Root Extracts. Phytother Res. 2009; 23:283-288.
26. Valentao P, Fernndes E, Canvalho E, Andrade PB, Seabra RM, Bastos ML Antioxidant activity of Hypericumandrosaeniuminfusion scavenging effect on superoxide radical, hydroxyl radical and hypochlorous acid. Biol. Pharm. Bull. 2002; 25:1324-1327
27. Adkins WK, Taylor AE. Role of xanthine oxidase and neutrophils in ischemia–reperfusion injury in rabbit lung. J. Appl. Physiol. 1990; 69(6):2012-2018.
28. Romagnoli M, Gomez-Cabrera MC, Perrelli MG, Biasi F, Pallardó FV, Sastre J, Poli G, Viña J. Xanthine oxidase-induced oxidative stress causes activation of NF-κB and inflammation in the liver of type I diabetic rats. Free. Radic. Biol. Med. 2010; 49(2):171-177.
29. Hamanaka H, Mizutani H, Nouchi N, Shimizu Y, Shimizu M. Allopurinol hypersensitivity syndrome: hypersensitivity to oxypurinol but not allopurinol. Clin. Exp. Dermatol.. 1998; 23:32-34.
30. Borges F, Fernandes E, Roleira F. Progress towards the discovery of xanthine oxidase inhibitors. Curr. Med. Chem. 2002; 9:195-217.
31. Abdullahi A , Hamzah RU, Jigam AA, Yahya A , Kabiru AY , Muhammad H, Sakpe S, Adefolalu FS, Isah MC, Kolo MZ. Inhibitory activity of xanthine oxidase by fractions Crateva adansonii. J. Acute Dis. 2012; 126-129.
32. Enroth C, Eger BY, Okamoto K., NishinoT, Pai EF. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. Natl. Acad. Sci. 2000; 97:10723.
33. Aruoma O I,. Free radicals, oxidative stress, and antioxidants in human health and disease. J. Amer. Oil Chem. Soc. 1998; 75:199-212.
Statistics
0 Views | 0 Downloads
How to Cite
1.
ZERARGUI F, SAFFIDINE K, GUEMMAZ T, BAGHIANI A. Inhibitory Effect of Xanthine Oxidase from Tamus communis Roots Extracts/Fraction. JDDT [Internet]. 15Oct.2020 [cited 21Oct.2020];10(5-s):164-9. Available from: http://jddtonline.info/index.php/jddt/article/view/4362