UDC 577.1:619                                                              http://dx.doi.org/10.15407/animbiol18.04.098

GLUTATHIONE-RELATED ENZYMES OF LIVER AND CAECUM OF ANIMALS

O. M. Fedets, I. M. Kurliak, R. S. Dankovych

This email address is being protected from spambots. You need JavaScript enabled to view it.

Stepan Gzhytsky Lviv National University
of Veterinary Medicine and Biotechnologies,
50 Pekarska str., Lviv 79010, Ukraine

The activities of glutathione S-transferase, glutathione peroxidase and glutathione reductase and the concentration of glutathione in liver and mucosa of caecum of cattle, guinea pig, horse, pig, rabbit and sheep have been investigated and compared.

Major differences were observed between the tested animals. The activity of glutathione S-transferase and level of glutathione were significantly higher in animals’ liver than in caecum. In liver the activity of glutathione S-transferase in order from high to low was as follows: sheep> rabbit > guinea pig > horse > pig > cattle. In caecum glutathione S-transferase activity was the highest in rabbit. In liver the level of glutathione was the highest in sheep and it was the lowest in cattle. The activity of glutathione peroxidase was significantly higher in liver of rabbit and pig than in their caecum. The lowest data were in both organs of horse. It was not detected in caecum of guinea pig. The activity of glutathione reductase was higher in animals’ caecum than in liver. The enzyme activity was higher in the liver only in the guinea pig.

The differences were significant in cattle, pig and horse but not in rabbit and guinea pig. The enzyme activity was similar in caecum of cattle and pig. The significant difference was between rabbit and horse. The investigations should be carried out on all animal species.

Keywords: GLUTATHIONE, GLUTATHIONE TRANSFERASE, GLUTATHIONE PEROXIDASE, GLUTATHIONE REDUCTASE, LIVER, CАECUM

1. Alin P., Jensson H., Guthenberg C., Danielson U. H., Tahir M. K., Mannervik B. Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing. Anal. Biochem., 1985, vol. 146, no. 2, pp. 313–320. https://doi.org/10.1016/0003-2697(85)90545-7

2. Beutler E., Duron O., Kelly B. M. Improved method for the determination of blood glutathione. J. Lab. Clin. Med., 1963, vol. 61, no. 5, pp. 882–888.

3. Carlberg I., Mannervik B. Purification and characterization of the flavoenzyme glutathione reductase from rat liver. J. Biol. Chem., 1975, vol. 250, no. 25, pp. 5475–5480.

4. Friess S. L. Critical issues facing animal scientists. J. Anim. Sci., 1983, vol. 56, no. 1, pp. 217–221. https://doi.org/10.2527/jas1983.561217x

5. Gusson F., Carletti M., Albo A. G., Dacasto M., Nebbia C. Comparison of hydrolytic and conjugative biotransformation pathways in horse, cattle, pig, broiler chicks, rabbit and rat liver subcellullar fractions. Vet. Res. Commun., 2006, vol. 30, no. 3, pp. 271–283. https://doi.org/10.1007/s11259-006-3247-y

6. Habig W. H., Pabst M. J., Jakoby W. B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem., 1974, vol. 249, no. 22, pp. 7130–7139.

7. Lhoste E. F., Ouriet V., Bruel S., Flinois J.-P., Brezillon C., Magdalou J., Cheze C., Nugon-Baudon L. The human colonic microflora influences the alterations of xenobiotic-metabolizing enzymes by catechins in male F344 rats. Food Chem. Toxicol., 2003, vol. 41, no. 5, pp. 695–702. https://doi.org/10.1016/S0278-6915(03)00010-3

8. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem., 1951, vol. 193, no. 1, pp. 265–275.

9. Nebbia C. Biotransformation enzymes as determinants of xenobiotic toxicity in domestic animals. Vet. J., 2001, vol. 161, I. 3, pp. 238–252.

10. Ogasawara T., Hoensch H., Ohnhaus E. E. Distribution of glutathione and its related enzymes in small intestinal mucosa of rats. Arch Toxicol. Suppl., 1985, vol. 8, pp. 110–113. https://doi.org/10.1007/978-3-642-69928-3_13

11. Pirie A. Glutathione peroxidase in lens and a source of hydrogen peroxide in aqueous humour. Biochem. J., 1965, vol. 96, pp. 244–253. https://doi.org/10.1042/bj0960244

12. Pompella A., Visvikis A., Paolicchi A., de Tata V., Casini A. F. The changing faces of glutathione, a cellular protagonist. Biochem. Pharmacol., 2003, vol. 66, I. 8, pp. 1499–1503.

13. Samiec P. S., Dahm L. J., Jones D. P. Glutathione S-transferase in mucus of rat small intestine. Toxicol. Sci., 2000, vol. 54, no. 1, pp. 52–59. https://doi.org/10.1093/toxsci/54.1.52

14. Sivapathasundaram S., Sauer M. J., Ionnides C. Xenobiotic conjugation systems in deer compared with cattle and rat. Comp. Biochem. Physiol., 2003, vol. 134, no. 1, pp. 169–173. https://doi.org/10.1016/S1532-0456(02)00224-7

15. Smith G. S., Watkins J. B., Thompson T. N., Rozman K., Klaassen C. D. Oxidative and conjugative metabolism of xenobiotics by livers of cattle, sheep, swine and rats. J. Anim. Sci., 1984, vol. 58, no. 2, pp. 386–395. https://doi.org/10.2527/jas1984.582386x

16. Szotakova B., Baliharova V., Lamka J., Nozinova E., Wsol V., Velik J., Machala M., Neca J., Soucek P., Susova S., Skalova L. Comparison of in vitro activities of biotransformation enzymes in pig, cattle, goat and sheep. Res. Vet. Sci., 2004, vol. 76, I. 1, pp. 43–51.

17. Tahir M. K., Ozer N., Mannervik B. Isoenzymes of glutathione transferase in rat small intestine. Biochem. J., 1988, vol. 253, I. 3, pp. 759–764.

18. Watkins J. B., Klaassen C. D. Xenobiotic biotransformation in livestock: comparison to other species commonly used in toxicity testing. J. Anim. Sci., 1986, vol. 63, pp. 933–942. https://doi.org/10.2527/jas1986.633933x

19. Watkins J. B., Smith G. S., Hallford D. M. Characterization of xenobiotic biotransformation in hepatic, renal and gut tissues of cattle and sheep. J. Anim. Sci., 1987, vol. 65, pp. 186–195. https://doi.org/10.2527/jas1987.651186x

20. Virkel G., Carletti M., Cantiello M., Della Donna L., Gardini G., Girolami F., Nebbia C. Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa. J. Vet. Pharmacol. Ther., 2010, vol. 33, I. 3, pp. 295–303.

Download full text in PDF format

Search