Identification of the Catalytic Site of Rat Liver Glutathione Peroxidase as Selenocysteine†

Biochemistry

Volumn 17, Issue 13, 1978, Pages 2639-2644

  Forstrom, John W ^a   Zakowski, Jack J ^a   Tappel, A L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; SELENOCYSTEINE;

ANIMAL EXPERIMENT; GLUTATHIONE PEROXIDASE SE 75; LIVER; RAT;

AMINO ACIDS; ANIMAL; BINDING SITES; CYSTEINE; GLUTATHIONE PEROXIDASE; LIVER; PEROXIDASES; RATS; SELENIUM; SPECTRUM ANALYSIS, MASS; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0017889205     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00606a028     Document Type: Article

References (54)

1. Andreeson, J. R., and Ljungdahl, L. G. (1973), J. Bacteriol. 116, 867.
2. Brenner, M., and Niederwieser, A. (1967), Methods Enzymol. 11, 39.
3. Burk, R. F. (1976), in Trace Elements in Human Health and Disease, Vol. II, Prasad, A. S., Ed., New York, N.Y., Academic Press, p 243.
4. Cantor, A. H., Langevin, M., Noguchi, T., and Scott, M. L. (1975a), J. Nutr. 105, 106.
5. Cantor, A. H., Scott, M. L., and Noguchi, T. (1975b), J. Nutr. 105, 96.
6. Cary, E. L., Allaway, W. H., and Miller, M. (1973), J. Anim. Sci. 36, 285.
7. Cavallini, D., DeMarco, D., Mondovi, B., and Azzone, G. F. (1955), Experientia 11, 61.
8. Chiu, D., Tappel, A. L., and Millard, M. M. (1977), Arch. Biochem. Biophys. 184, 209.
9. Combs, G. F., Jr., Noguchi, T., and Scott, M. L. (1975), Fed. Proc., Fed. Am. Soc. Exp. Biol. 34, 2090.
10. Cone, J. E., Del Rio, R. M., Davis, J. N., and Stadtman, T. C. (1976), Proc. Natl. Acad. Sci. U.S.A. 73, 2659.
11. Cummins, L. M., and Martin, V. L. (1967), Biochemistry 6, 3162.
12. Davis, B. J. (1964), Ann. N.Y. Acad. Sci. 121, 404.
13. Diplock, A. T., Baum, H., and Lucy, J. A. (1971), Biochem. J. 123, 721.
14. Enoch, H. G., and Lester, R. L. (1972), J. Bacteriol. 110, 1032.
15. Enoch, H. G., and Lester, R. L. (1975), J. Biol. Chem. 250, 6693.
16. Fletcher, B. L. (1975), M.S. Thesis, University of California, Davis, Calif.
17. Flohé, L., and Günzler, W. A. (1974), in Glutathione, Flohé, L., Benöhr, H. Ch., Sies, H., Waller, H. D., and Wendel, A., Ed., New York, N.Y., Academic Press, p 132.
18. Flohé, L., Günzler, W. A., and Ladenstein, R. (1976), in Glutathione, Vol. 6, Arias, I. M., and Jakoby, W. B., Ed., New York, N.Y., Raven Press, p 115.
19. Flohé, L., Günzler, W. A., and Schock, H. H. (1973), FEBS Lett. 32, 132.
20. Flohé, L., Schaich, E., Voelter, W., and Wendel, A. (1971), Hoppe-Zeyler's Z. Physiol. Chem. 352, 170.
21. Flohé, L., and Zimmerman, R. (1970), Biochim. Biophys. Acta 223, 210.
22. Ganther, H. E. (1974), in Selenium, Zingaro, R. A., and Cooper, W. C., Ed., New York, N.Y., Van Nostrand Reinhold Co., p 546.
23. Ganther, H. E., Hafeman, D. G., Lawrence, R. A., Serfass, R. E., and Hoekstra, W. G. (1976), in Trace Elements in Human Health and Disease, Vol. II, Prasad, A. S., Ed., New York, N.Y., Academic Press, p 165.
24. Heath, R. L., and Tappel, A. L. (1976), Anal. Biochem. 76, 184.
25. Hoekstra, W. G. (1975), Fed. Proc., Fed. Am. Soc. Exp. Biol. 34, 2083.
26. Hsieh, H. S., and Ganther, H. E. (1975), Biochemistry 14, 1632.
27. Hsu, C. K. (1976), M.S. Thesis, University of California, Davis.
28. Huber, R. E., and Criddle, R. S. (1967), Arch. Biochem. Biophys. 122, 164.
29. Huovinen, J. A. (1968), Ann. Med. Exp. Fenn. 46, 89.
30. Irgolic, K. J., and Kudchadker, M. V. (1974), in Selenium, Zingaro, R. A., and Cooper, W. C., Ed., New York, N.Y., Van Nostrand Reinhold Co., p 408.
31. Jenkins, K. J. (1968), Can. J. Biochem. 46, 1417.
32. Little, C., and O'Brien, P. J. (1968), Biochem. Biophys. Res. Commun. 31, 145.
33. McConnell, K. P., and Wabnitz, C. H. (1957), J. Biol. Chem. 226, 765.
34. Mills, G. C. (1959), J. Biol. Chem. 234, 502.
35. Morris, H. R., Williams, D. H., and Ambler, R. P. (1971), Biochem. J. 125, 189.
36. Nakamura, W., Hosoda, S., and Hayashi, K. (1974), Biochim. Biophys. Acta 358, 251.
37. Ochoa-Solano, A., and Gitler, C. (1968), J. Nutr. 94, 243.
38. Oh, S.-H., Ganther, H. E., and Hoekstra, W. G. (1974), Biochemistry 13, 1825.
39. Olson, E. O., and Palmer, S. (1976), Metabolism 25, 299.
40. Ornstein, L. (1964), Ann. N. Y. Acad. Sci. 121, 321.
41. Pinsent, J. (1954), Biochem. J. 57, 10.
42. Prohaska, J. R., Oh, S.-H., Hoekstra, W. G., and Ganther, H. E. (1977), Biochem. Biophys. Res. Commun. 74, 64.
43. Raftery, M. A., and Cole, R. D. (1963), Biochem. Biophys. Res. Commun. 10, 467.
44. Rhead, W. J., and Schrauzer, G. N. (1974), Bioinorg. Chem. 3, 225.
45. Rotruck, J. T., Pope, A. L., Ganther, H. E., Swanson, A. B., Hafeman, D. G., and Hoekstra, W. G. (1973), Science 179, 588.
46. Schwarz, K., and Foltz, C. M. (1958), J. Biol. Chem. 233. 245.
47. Schwarz, K., and Fredga, A. (1969), J. Biol. Chem. 244, 2103.
48. Stults, F. H., Forstrom, J. W., Chiu, D. T. Y., and Tappel, A. L. (1977), Arch. Biochem. Biophys. 183, 490.
49. Tappel, A. L. (1974), Am. J. Clin. Nutr. 27, 960.
50. Turner, D. C., and Stadtman, T. C. (1973), Arch. Biochem. Biophys. 154, 366.
51. Udenfriend, S., Stein, S., Bohlen, P., Dairman, W., Leimgruber, W., and Weigele, M. (1972), Science 178, 871.
52. Wendel, A., Pilz, W., Ladenstein, R., Sawatski, G., and Weser, U. (1975), Biochim. Biophys. Acta 377, 211.
53. Whatkinson, J. H. (1966), Anal. Chem. 38, 92.
54. Wu, G. J., and Breuning, G. (1971), Virology 46, 596.