In Vitro Oxidation of the Hydrolysis Product of Sulfur Mustard, 2,2′-Thiobis-ethanol, by Mammalian Alcohol Dehydrogenase

Journal of Biochemical and Molecular Toxicology

Volumn 12, Issue 6, 1998, Pages 361-369

  Brimfield, A A ^a   Zweig, L M ^a   Novak, M J ^a   Maxwell, D M ^a  

^a US ARMY MEDICAL RESEARCH INSTITUTE OF CHEMICAL DEFENSE   (United States)

Author keywords

2,2 Thiobis ethanol; Alcohol Dehydrogenase; Oxidative Metabolism; Skin; Sulfur Mustard; Thiodiglycol

Indexed keywords

EQUUS CABALLUS; MAMMALIA;

ALCOHOL DEHYDROGENASE; ENZYME INHIBITOR; MUSTARD GAS; NICOTINAMIDE ADENINE DINUCLEOTIDE;

ANIMAL; ARTICLE; CYTOSOL; DRUG ANTAGONISM; ENZYME SPECIFICITY; HORSE; HUMAN; HYDROLYSIS; LIVER; METABOLISM; MOUSE; OXIDATION REDUCTION REACTION; SKIN;

ALCOHOL DEHYDROGENASE; ANIMALS; CYTOSOL; ENZYME INHIBITORS; HORSES; HUMANS; HYDROLYSIS; LIVER; MICE; MUSTARD GAS; NAD; OXIDATION-REDUCTION; SKIN; SUBSTRATE SPECIFICITY;

EID: 0031615936     PISSN: 10956670     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-0461(1998)12:6<361::aid-jbt6>3.0.co;2-z     Document Type: Article

References (27)

1. J. C. Dacre and M. Goldman (1996). Toxicology and pharmacology of the chemical warfare agent sulfur mustard. Pharmacol. Rev., 48(2), 289-320.
2. B. Papirmeister, A. J. Fiester, S. I. Robinson, and R. D. Ford (1991). Medical Defense against Mustard Gas, 359 pp., CRC Press, Boca Raton, FL.
3. Y.-M. Li and J. E. Casida (1992). Cantharidin-binding protein: Identification as protein phosphatase 2A, Proc. Natl. Acad. Sci. U.S.A., 89, 11867-11870.
4. 3H]endothall thioanhydride binding site, Biochem. Pharmacol., 46(8), 1435-1443.
5. R. Eldridge and J. E. Casida (1995). Cantharidin effects on protein phosphatases and the phosphorylation state of phosphoproteins in mice, Toxicol. Appl. Pharmacol., 130, 95-100.
6. C. F. B. Holmes and M. P. Boland (1993). Inhibitors of protein phosphatase-1 and -2A; two of the major serine/ threonine protein phosphatases involved in cellular regulation, Curr. Opin. Struct. Biol., 3, 934-943.
7. A. Takai and G. Mieskes (1991). Inhibitory effect of okadaic acid on p-nitrophenylphosphate phosphatase activity of protein phosphatases, Biochem. J., 275, 233-239.
8. A. A. Brimfield (1995). Possible protein phosphatase inhibition by bis(hydroxyethyl) sulfide, a hydrolysis product of mustard gas, Toxicol. Lett., 78, 43-48.
9. P. D. Bartlett and C. G. Swain (1949). Kinetics of hydrolysis and displacement reactions of β,β′-dichlorodiethyl sulfide (mustard gas) and of β-chloro-β-hydroxy diethyl sulfide (mustard chlorohydrin), J. Am. Chem. Soc., 71, 1406-1415.
10. A. A. Brimfield (1996). Progress in the investigation of protein phosphatase inhibition by thiodiglycol, Proceedings of the 1996 Medical Defense Bioscience Review, vol. II, pp. 675-683, Accession Number A321841, U.S. Army Medical Research Institute of Chemical Defense, Defense Technical Information Center, Cameron Station, Alexandria, VA 22304-6145.
11. A. A. Brimfield, L. A. Cook, M. J. Novak, and D. M. Maxwell (1997). In vitro metabolic oxidation of thiodiglycol, the hydrolysis product of sulfur mustard, by alcohol dehydrogenase, The Toxicologist, 36(1), part 2, 318.
12. M. Madesclaire (1986). Synthesis of sulfoxides by oxidation of thioethers, Tetrahedron, 42, 5459-5495.
13. M. J. Graziano, I. N. Pessah, M. Matzuzawa, and J. E. Casida (1988). Partial characterization of specific cantharidin binding sites in mouse tissues, Mol. Pharmacol., 33, 706-712.
14. O. H. Lowrey, N. J. Rosebrough, and A. L. Farr (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275.
15. R. B. McComb, L. W. Bond, R. W. Burnett, R. C. Keech, and G. N. Bowers (1976). Determination of the molar absorptivity of NADH. Clin. Chem., 22, 141-150.
16. M. Dixon (1953). The determination of enzyme inhibitor constants, Biochem. J., 55, 170-171.
17. R. M. Black, K. Brewster, R. J. Clarke, J. L. Hambrook, J. M. Harrison, and D. J. Howells (1993). Metabolism of thiodiglycol (2,2′-thiobis-ethanol): Isolation and identification of urinary metabolites following intraperitoneal administration to rat. Xenobiotica, 23, 473-481.
18. R. M. Black, J. L. Hambrook, D. J. Howells, and R. W. Read (1992). Biological fate of sulfur mustard, 1,1′-thiobis(2-chloroethane). Urinary excretion profiles of hydrolysis products and β-lyase metabolites of sulfur mustard after cutaneous application in the rat. J. Anal. Toxicol., 16, 79-84.
19. R. M. Black, K. Brewster, R. J. Clarke, J. L. Hambrook, J. M. Harrison, and D. J. Howells (1992). Biological fate of sulfur mustard, 1,1′-thiobis(2-Chloroethane): Isolation and identification of urinary metabolites following intraperitoneal administration to rat. Xenobiotica, 22, 405-418.
20. P. V. Taberner, J. T. Rick, and G. A. Kerkut (1972). Metabolic factors involved in the interaction between pyrazole and butane-1,4-diol and hydroxybutyric acid. Life Sci., 11(Part I), 335-341.
21. M. Reynier (1969). Pyrazole inhibition and kinetic studies of ethanol and retinol oxidation catalyzed by rat liver alcohol dehydrogenase. Acta Chem. Scan., 23, 1119-1129.
22. W. F. Bosron, T.-K. Li, W. P. Dafeldecker, and B. L. Vallee (1979). Human liver π-alcohol dehydrogenase: Kinetic and molecular properties. Biochemistry, 18, 1101-1105.
23. K. C. Posch and J. L. Napoli (1992). Multiple retinoid dehydrogenases in testes cytosol from alcohol dehydrogenase negative or positive deermice. Biochem. Pharmacol., 43, 2296-2298.
24. Y. Morita (1955). d-trans-7-Aldehydo-π-apocamphor. I. Its effect on dehydrogenase activities in comparison with other aldehydes. Folia Pharmacol. Japon., 51, 91-93.
25. C. Davison, R. S. Rozman, and P. K. Smith (1961). Metabolism of bis-beta-chloroethyl sulfide (sulfur mustard gas). Biochem. Pharmacol., 7, 65-74.
26. E. Hodgson and P. E. Levi (1988). The flavin-containing monooxygenase as a sulfur oxidase. In Metabolism of Xenobiotics, J. W. Gorrod, H. Oelschlager, and J. Caldwell, eds., pp. 81-88, Taylor and Francis, London.
27. P. E. Levi and E. Hodgson (1988). Stereospecificity in the oxidation of phorate and phorate sulfoxide by purified FAD-containing monooxygenase and cytochrome P-450 isozymes. Xenobiotica, 18, 29-34.