In-vitro and in-vivo studies on the effect of cystamine and sodium thiosulfate on cyanide detoxification mediated by rhodanese

Iranian Journal of Science and Technology, Transaction B: Technology

Volumn 27, Issue 1, 2003, Pages 175-184

  Aminlari, M ^a   Zohrabi, A ^a  

^a SHIRAZ UNIVERSITY   (Iran)

Author keywords

Cyanide toxicity; Cystamine; Disulfides; DTNB; Rhodanese

Indexed keywords

METABOLISM; ORGANIC ACIDS; TOXIC MATERIALS;

CYSTINE;

CHEMICAL REACTIONS;

CYANIDE;

EID: 0038638547     PISSN: 03601307     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (32)

1. Lang, K., Die rhodanbildung in tierkorper, Biochem. Z., 259, p. 243 (1933).
2. Himwich, W. A. and Saunders, J. P., Enzymatic conversion of cyanide to thiocyanate, Am. J. Physiol., 153, p. 348 (1948).
3. Koj, A. and Frendo, J., The activity of cyanide desulpdrase and rhodanese in animals tissues, Acta Biochem. Pol. 9, p. 373 (1962).
4. Wood, J. L., Biochemistry of Thiocyanic Acid, In Chemistry and Biochemistry of Thiocyanic Acid and Its Derivatives (Edited by Newmann, A.A.), p. 156, Academic Press, New York (1975).
5. Drawbaugh, R. B. and Marrs, T. C., Interspecies differences in rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) activity in liver, kidney, and plasma, Comp. Biochem. Physio., 86B, p. 307 (1987).
6. Frankenberhg, L., Enzyme therapy in cyanide poisoning: Effect of rhodanese and sulfur compound, Arch Thoxicol, 45, p. 315 (1980).
7. Westely, J., Cyanide and Sulfane Sulfur, In: Cyanide in Biology, (Vennesland, B., Conn, E. E., Knowles, C. J., Westley, J. and Wissing, F., eds.), p. 61, Academic Press, New York (1981).
8. Calabrese, E. J., Cyanide toxicity, In Principles of Animal Extrapolation, p. 278, Wiley, New York (1983).
9. Egekeze, J. O. and Oehme, F. W., Cyanides and their toxicity: A literature review, Vet. Quat., 2, p. 104 (1980).
10. Leung, P., Ray, L. E., Sander, C., Way, Jon L., Sylvester, D. M. and Way, J. L., Encapsulation of thiosulfate: cyanide sulfurtransferase by mouse erythrocytes, Toxicol. Appl. Pharmacol., 83, p. 101 (1986).
11. Aminlari, M., Vaseghi, T. and Kargar, M. A., The cyanide metabolizing enzyme rhodanese in different parts of the respiratory system of sheep and dog, Toxicol. Appl. Pharmacol., 124, p. 67 (1994).
12. Aminlari, M., Gholami, S., Vaseghi, T. and Azarafrooz, A. Rhodanese (thiosulfate: cyanide sulfurtransferase) in the digestive tract of chicken at different stages of development. Poult. Sci., 76, p. 318 (1997).
13. Pagani, S., Bonomi, F. and Cerletti, P., Sulfide insertion into spinach ferredoxin by rhodanese, Biochim. Biophys. Acta., 700, p. 154 (1982).
14. Ogata, K., Dai, X. and Volini, M., Bovine liver mithochondrial rhodanese is a phosphoprotein, J. Biol. Chem., 264, p. 2718 (1989).
15. Sorbo, B. H., Crystalline rhodanese. I. Purification and physicochemical examination, Acta Chem. Scand., 7, p. 1129 (1953).
16. Ploegman, T. H., Drent, G., Kalk, K. H., Hol, W. G. J., Heinrikson, R. L., Klein, P., Weng, L. and Russell, J. The covalent and tertiary structure of bovine liver rhodanese, Nature, 273, p. 124 (1978a).
17. Russell, J., Weng, L., Klein, P. S. and Heinrikson, R. L., The covalent structure of bovine liver rhodanese. Isolation and partial structural analysis of cyanogen bromide fragments and the complete sequence of the enzyme, J. Biol. Chem., 253, p. 8102 (1978).
18. Weng, L., Heinrikson, R. L. and Westely, J., Active site cysteinyl and arginyl residues of rhodanese, A novel formation of disulfide bonds in the active site promoted by phenylglyoxal, J. Biol. Chem. 253, p. 8109 (1978).
19. Wilson, J. M., Wu, D., Motiu-DeGrood, R. and Hupe, D. J., A spectrophotometric method for studying the rates of reaction of disulfides with protein thiol groups applied to bovine serum albumin, Amer. Chem. Soc., 102, p. 359 (1980).
20. Horowitz, P. and DeToma F., Improved preparation of bovine liver rhodanese, J. Biol. Chem., 245, p. 984 (1970).
21. Schelesinger, P. and Westley, J., An expanded mechanism for rhodanese catalysis, J. Biol. Chem., 249, p. 780 (1974).
22. Horowitz, P. and Crisamagana, N., The use of intrinsic protein flourescence to quantitate enzyme-bound persulfide and to measure equilibrium between intermediates in rhodanese catalysis, J. Biol. Chem., 258, p. 7894 (1983).
23. Wang, S. F. and Volini, M., Studies on the active site of rhodanese, J. Biol. Chem., 243, p. 5465 (1968).
24. Ellman, G. L., Tissue sulfhydryl groups, Arch. Biochem. Biophys., 82, p. 70 (1959).
25. Grassetti, D. R., and Murray, J. F., Determination of sulfhydryl groups with 2,2'- or 4,4'-dithiodipyridine. Arch. Biochem. Biophys., 119, p. 41 (1967).
26. Pensa, B., Costa, M., Pecci, L., Canella, C. and Cavalini, D., Selective reactivity of rhodanese sulfhydryl groups with 5,5'-dithiobis (2-nitrobenzoic acid), Biochim. Biophys. Acta., 484, p. 368 (1977).
27. Wilson, J. M., Baxer, R. J. and Hupe, D. J., Structure-reactivity correlation for thiol-disulfide interchange reaction, J. Amer. Chem. Soc., 99, p. 7922 (1977).
28. Whitesides, G. M., Lilburn, J. E. and Szajewski, R. P., Rates of thiol-disulfide interchange reactions between mono-and dithiol and Ellman's reagent, J. Org. Chem., 42, p. 332 (1977).
29. Ploegman, J. H., Drent, G., Kalk, K. H. and Hol, W. G. J., Structure of bovine liver rhodanese. I. Structure determination at 2.5 A° resolution and a comparison of the conformation and sequence of its two domains, J. Mol. Biol., 123, p. 557 (1978b).
30. Osuga, D. T., Aminlari, M., Ho, C. Y. K., Allison, R.G. and Feeney, R. E. Sulfhydryl proteins of penguin egg white: ovalbumin and penalbumin, Comparison with penguin serum albumin, chicken ovalbumin, and bovine serum albumin, J. Protein Chem., 2, p. 43 (1983).
31. Westely, J. Rhodanese, Adv. Enzymol., 39, p. 327 (1973).
32. Szczepkowski, T. W. and Wood, J. L., The cystathionase rhodanese system, Biochim. Biophys. Acta., 139, p. 469 (1967).