Superoxide dismutase and catalase activites in erythrocytes and plasma from patients with rheumatoid arthritis

7. SUMMARY In the present study, antioxidant enzyme activities such as superoxide dismutase (SOD) and catalase (CAT) were determined in erythrocytes and plasma taken from the patients with rheumatoid arthritis. The patients were divided into two groups; group 1 received the classical treatment (n= 26) and group 2 no treatment for rheumatoid arthritis. SOD activity was determined via xanthine/xanthine oxidase system. CAT activity was determined by the decrease of H2O2 absorbance at ultraviolet spectrum. In the determination of SOD activity, the ethanol/chloroform extraction (w/w, 5/3) was also used to prevent the artefacts originated from the red colour of haemoglobin. The results were compared with enzyme activities of the control group (11= 22). No catalase activity was determined in the plasma taken from both the patient groups and the control groups. Erythrocyte SOD activity was 1 184 ± 182 U/g Hb and CAT activity was 66,7 ± 14,6 K/gr Hb in the patients with rheumatoid arthritis receiving classical treatment (Group I). In group 2, receiving no treatment for rheumatoid arthritis, SOD and CAT activity were 1220,0 ±214,6 U/gr Hb and 67,4 ± 16.8 K/gr Hb respectively. Plasma SOD activity in this group was 1,35 ± 0,88 U/ml (p < 0,05). In control group erythrocyte SOD and CAT activities were 1 194 ± 172.4 U/gr Hb and 62,6 ± 15,9 K/gr Hb respectively and plasma SOD activity was 2,39 ± 0,87 U/mL. As seen, diminishing of plasma SOD activity was significant in the patient group receiving no treatment. The results of the study were discussed in considering literature. As a conclusion, it has suggested that antioxidant enzymes do not play an important role in the etiology of anemia in rheumatoid arthritis, because no significant enzyme activity was determined when compared with control group in our study. 428. KAYNAKLAR 1. Slater T.F. Free radicals and tissue injury. Biochem J. 1984; 222: 1-15 2. Kılınç K. Oksijen Radikalleri: Üretilmeleri, Fonksiyonları ve Toksik Etkileri, Biyokimya Dergisi 1985; 10 (2): 60-89. 3 Sies H. Role of reactive oxygen species in biological processes. Clin Wochenschr 1991;69:965-968. 4. Fridovich I. Superoxide dismutases. Ann. Rev. Biochem 1975, 44: 147-159. 5. Fridovich I. Superoxide radical: An endogenous toxicant. Ann Rev. Pharmacol Toxicol. 1983;23:239-57. 6. Aleman V. and Handler P. Dihydroorotate dehydrogenose. The Journal of Biological Chemistry. 1967; 242 (18): 4087-4096. 7. Turrens J.F. and Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J. 1980; 191:421-427. 8. Fi idowich 1. Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. The Journal of Biological Chemistry. 1970; 25: 4053- 4057. 9. Sohal R.S., and Brunk U.T. Mitokondrial pruduction of prooxidants and cellular senescense. Mutation Research. 1992; 275: 295-304. lO.Sothorn PA, Powis G. Free radicals in medicine. I. chemical nature and biologic reactions. Mayo Clin Proc. 1988; 63: 381-389. ll.Deby C. and Goutier R. New perspectives on the biochemistry of superoxide anion and the efficiency of superoxide dismutase. Biochemical Pharmacology. 1990;39:399-405. 12Auer D.E., NG CJ. and Seawright A.A. Effect of palosein (superoxide dismutase) and catalase upon oxygen derived free radical induced degradation of equine synavial fluid. Equine Veterinary Journal 1990; 22 (1): 13-17. 13.Britgan BE., Pou S., Rosen G.M., Lilleg D.M. and Buettner G.R. Hydroxyl radical is not a product of the reaction of xanthine oxidase and xanthine. The Journal of Biological Chemistry. 1990; 265 (29): 17533-17538..H