The influence of mercury on the antioxidant enzyme activity of rumen bacteria Streptococcus bovis and Selenomonas ruminantium

FEMS Microbiology Ecology

Volumn 27, Issue 4, 1998, Pages 319-325

  Lenártová, Viera ^a   Holovská, Katarína ^a   Javorský, Peter ^b  

^a UNIVERSITY OF VETERINARY MEDICINE   (Slovakia)

^b INSTITUTE OF ANIMAL PHYSIOLOGY   (Slovakia)

Author keywords

Antioxidant enzyme; Mercury; Selenomonas ruminantium; Streptococcus bovis

Indexed keywords

GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; MERCURY; SULFIDE; SUPEROXIDE DISMUTASE; THIOBARBITURIC ACID REACTIVE SUBSTANCE;

ANAEROBIC BACTERIUM; ANTIOXIDANT ACTIVITY; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; RUMEN MICROORGANISM; RUMINANT STOMACH; STREPTOCOCCUS BOVIS;

BACTERIA (MICROORGANISMS); SELENOMONAS RUMINANTIUM; STREPTOCOCCUS BOVIS;

EID: 17044446127     PISSN: 01686496     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6496(98)00077-4     Document Type: Article

References (41)

1. Stohs, S.J. and Bagchi, D. (1995) Oxidative mechanisms in the toxicity of metal ions. Free Radical Biol. Med. 18, 321-336.
2. Forsberg, C.W. (1978) Effects of heavy metals and other trace elements on the fermentative activity of the rumen microflora and growth of functionally important rumen bacteria. Can. J. Microbiol. 24, 298-306.
3. Luckey, T.D., Venugopal, B. and Hutcheson, D. (1975) Environmental Quality and Safety, Suppl. Vol. 1. Academic Press, New York.
4. Ribarov, S.R. and Benov, L.C. (1981) Relationship between the hemolytic action of heavy metals and lipid peroxidation. Biochim. Biophys. Acta 640, 721-726.
5. 2 production and lipid oxidation in vitro in rat kidney mitochondria. Biochem. Pharmacol. 42, 181-187.
6. Furukawa, K., Suzuki, T. and Tonomura, K. (1969) Decomposition of organic mercurial compounds by mercury-resistant bacteria. Agric. Biol. Chem. 33, 128-130.
7. Schottel, J.L. (1978) The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli. J. Biol. Chem. 253, 4341-4349.
8. Sahlman, L., Lambeir, A.M., Lindskog, S. and Dunford, H.B. (1984) The reaction between NADPH and mercuric reductase from Pseudomonas aeruginosa. J. Biol. Chem. 259, 12403-12408.
9. Hungate, R.E. (1966) The Rumen and its Microbes. Academic Press, New York.
10. Latham, M.J., Sharpe, M.E. and Sutton, J.D. (1971) The microbial flora of the rumen of cows fed hay and high cereal rations and its relationship to the rumen fermentation. J. Appl. Bacteriol. 34, 425-434.
11. Štyriak, I., Španová, A., Montagová, H. and Kmet', V. (1994) Isolation and characterization of a new ruminai bacteriophage lytic to Streptococcus bovis. Curr. Microbiol. 28, 355-358.
12. Pristaš, P., Vanat, I. and Javorský, P. (1997) Variability of endonucleolytic activity indicates high genetic diversity within the natural population of Selenomonas ruminantium. Folia Microbiol. 42, 121-124.
13. Tiwari, A.D., Bryant, M.P. and Wolfe, R.S. (1969) Simple method for isolation of Selenomonas ruminantium and some nutritional characteristics of the species. J. Dairy Sci. 52, 2054-2056.
14. Flohé, L. and Ötting, F. (1984) Superoxide dismutase assays. Methods Enzymol. 105, 93-104.
15. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
16. Beauchamp, C. and Fridovich, I. (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44, 276-278.
17. Briton, L., Malinowski, D.P. and Fridovich, I. (1978) Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms. J. Bacteriol. 135, 229-236.
18. Flohé, L. and Günzler, W.A. (1984) Assays of glutathione peroxidase. Methods Enzymol. 105, 114-121.
19. Pinto, M.C., Mata, A.M. and López-Barea, J. (1984) Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions. Arch. Biochem. Biophys. 228, 1-12.
20. Fox, B. and Walsh, C.T. (1982) Mercuric reductase. J. Biol. Chem. 257, 2498-2503.
21. Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
22. Gutteridge, J.M.C. (1984) Ferrous ion-EDTA-stimulated phospholipid peroxidation. Biochem. J. 224, 697-701.
23. Storz, G., Tartaglia, L.A., Farr, S.B. and Ames, B.N. (1990) Bacterial defences against oxidative stress. Trends Genet. 6, 363-368.
24. Chamnongpol, S., Mongkolsuk, S., Vattanaviboon, P. and Fuangthong, M. (1995) Unusual growth phase and oxygen tension regulation of oxidative stress protection enzymes, catalase and superoxide dismutase, in the phytopathogen Xanthomonas oryzae pv. oryzae. Appl. Environ. Microbiol. 61, 393-396.
25. Keele, B.B., McCord, J.M. and Fridovich, I. (1970) Superoxide dismutase from Escherichia coli B: a new manganese-containing enzyme. J. Biol. Chem. 245, 6176-6181.
26. Yost, F. and Fridovich, I. (1973) An iron-containing superoxide dismutase from Escherichia coli B. J. Biol. Chem. 248, 4905-4908.
27. Imlay, K.R.C. and Imlay, J.A. (1996) Cloning and analysis of sod C encoding the copper-zinc superoxide dismutase of Escherichia coli. J. Bacteriol. 178, 2564-2571.
28. Hopkin, K.A., Pappayian, A. and Steinman, H.M. (1992) Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12. J. Biol. Chem. 267, 2453-2458.
29. Hassan, H.M. and Schrum, L.W. (1994) Roles of manganese and iron in the regulation of the biosynthesis of manganese-superoxide dismutase in Escherichia coli. FEMS Microbiol. Rev. 14, 315-324.
30. Chang, S.K. and Hassan, H.M. (1997) Characterization of superoxide dismutase in Streptococcus thermophilus. Appl. Environ. Microbiol. 63, 3732-3735.
31. Goyer, R.A. (1991) Toxic effects of metals. In: Casarett and Doull's Toxicology: The Basic Science of Poisons (Amdur, M.O., Doull, J. and Klassen, C.D., Eds.), 4th edn., pp. 629-681. Pergamon Press, New York.
32. Gwozdinski, K., Roche, H. and Peres, G. (1992) The comparison of the effects of heavy metal ions on the antioxidant enzyme activities in human and fish Dicantrarchus labrax erythrocytes. Comp. Biochem. Physiol. 102C, 57-60.
33. Pennincx, M.J. and Elskens, M.T. (1993) Metabolism and functions of glutathione in micro-organisms. Adv. Microbiol. Physiol. 34, 269-271.
34. Lawrence, R.A. and Burk, R.F. (1978) Species, tissue and subcellular distribution of non Se-dependent glutathione peroxidase activity. J. Nutr. 108, 211-215.
35. Chung, A.S., Maines, M.D. and Reynolds, W.A. (1982) Inhibition of the enzymes of glutathione metabolism by mercuric chloride in the rat kidney: Reversal by selenium. Biochem. Pharmacol. 31, 3093-3100.
36. Yonaha, M., Saito, M. and Sagai, M. (1983) Stimulation of lipid peroxidation by methyl mercury in rats. Life Sci. 32, 1507-1514.
37. Zaman, K., MacGill, R.S., Johnson, J.E., Ahmad, S. and Pardini, R.S. (1994) An insect model for assessing mercury toxicity: Effect of mercury on antioxidant enzyme activities of the housefly (Musca domestica) and the cabbage looper moth (Trichoplusia ni). Arch. Environ. Contam. Toxicol. 26, 114-118.
38. Blaghen, M., El Kebba, M.S., Vidon, D.J.M. and Tritsch, D. (1992) Essential arginines in mercuric reductase isolated from Yersinia enterocolitica 138A 14. Biochimie 74, 557-560.
39. Finegold, S.M. and George, W.L. (1989) Anaerobic Infections in Humans. Academic Press, San Diego, CA.
40. Morris, J.G. (1980) Oxygen tolerance/intolerance of anaerobic bacteria. In: Anaerobes and Anaerobic Infections. Symposium held at the XII. International Congress of Microbiology in Munich, 3-8 September 1978 (Gottschalk, G., Penning, N. and Werner, H., Eds.), pp. 7-15. Gustav Fisher Verlag, Stuttgart.
41. Bray, A.C. and Till, A.R. (1975) Metabolism of sulphur in the gastro-intestinal tract. In: Digestion and Metabolism in the Ruminant (McDonald, I.W. and Warner, A.C.I., Eds.), pp. 243-260. The University of New England Publishing Unit, Armidale.