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International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine Volume 52, 1987 - Issue 3
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Original Article

Zinc Release from Irradiated Yeast Alcohol Dehydrogenase

S. Abelidis Department of Biological Sciences, University of Salford, Salford, M5 4WT, U.K.
,
J.S. Moore Department of Biological Sciences, University of Salford, Salford, M5 4WT, U.K.
&
A. Chakravarty Department of Biological Sciences, University of Salford, Salford, M5 4WT, U.K.
Pages 413-418 | Received 06 Apr 1987, Accepted 18 May 1987, Published online: 03 Jul 2009

References

  • Adams G.E., Aldrich J.E., Bisby R.H., Cundall R.B., Redpath J.L., Willson R.L. Selective free radical reactions with proteins and enzymes: reactions of inorganic radical anions with amino acids. Radiation Research 1972; 49: 278–289
  • Adams G.E., Baverstock K.F., Cundall R.B., Redpath J.L. Radiation effects on α-chymotrypsin in aqueous solution: pulse radiolysis and inactivation studies. Radiation Research 1973; 54: 375–387
  • Badiello R., Tamba M., Quintiliani M. Primary and secondary radicals in the radiation-induced inactivation of yeast alcohol dehydrogenase. International Journal of Radiation Biology 1974; 26: 311–319
  • Brändén C.I., Jörnvall H., Eklund H., Furugren B. Alcohol Dehydrogenases. The Enzymes, P.D. Boyer. Academic Press, New York 1975; 11: 103–190
  • Dainton F.S., Watt W.S. pH Effects in the γ-radiolysis of aqueous solutions. Proceedings of the Royal Society of London, Series A 1963; 275: 447–464
  • Gorin G., Quintiliani M., Airee S.K. The inactivation of alcohol dehydrogenase by X-rays and the dose-modifying effect of some added substances. Radiation Research 1967; 32: 671–684
  • Harris I. Structure and catalytic activity of alcohol dehydrogenases. Nature 1964; 203: 30–34
  • Hayes J.E., Velick S.F. Yeast alcohol dehydrogenase, molecular weight, coenzyme binding and reaction equilibria. Journal of Biological Chemistry 1954; 207: 225–244
  • Hiller K.O., Asmus K.D. Oxidation of methionine by X-2 in aqueous solution and characterization of some > S.·.X three electron bonded intermediates. A pulse radiolysis study. International Journal of Radiation Biology 1981; 40: 583–595
  • Jörnvall H., Woenckhaus C., Johnscher G. Modification of alcohol dehydrogenases with a reactive coenzyme analogue. European Journal of Biochemistry 1975; 53: 71–81
  • Kagi J.H.R., Vallee B.L. The role of zinc in alcohol dehydrogenase. Journal of Biological Chemistry 1960; 235: 3188–3192
  • Lutstorf U., Megnet R. Multiple forms of alcohol dehydrogenase in Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics 1968; 126: 933–944
  • Mahler R.H., Douglas J. Mechanisms of enzyme-catalysed oxidation—reduction reaction. I. An investigation of the yeast alcohol dehydrogenase reaction by means of the isotope effect. Journal of the American Chemical Society 1957; 79: 1159–1165
  • Prütz W.A., Butler J., Land E.J. Methionyl→tyrosyl radical transitions initiated by Br-2 in peptide model systems and ribonuclease A. International Journal of Radiation Biology 1985; 47: 149–156
  • Quintiliani M., Shejbal J., Davies J.V., Ebert M., Gilbert C.W. Reactions of radiation-induced I, I-2 and I-3 with alcohol dehydrogenase and aldolase. International Journal of Radiation Biology 1973; 24: 243–255
  • Roberts P.B. A radiolysis study of the inactivation and active site of carboxypeptidase A. International Journal of Radiation Biology 1973; 24: 143–152
  • Schimazu F., Tappel A.L. Selenoamino acids as radiation protectors in vitro. Radiation Research 1964; 23: 210–217
  • Schimpfessel L. Presence and regulation of the synthesis of two alcohol dehydrogenases in yeast. Internationales de Physiologie et de Biochemie 1967; 75: 368–369
  • Sloan D.L., Young J.M. Nuclear relaxation studies of the role of metals in yeast and liver alcohol dehydrogenase. Federation Proceedings 1974; 33: 1244–1244
  • Sund H., Theorell H. Alcohol dehydrogenases. The Enzymes, P.D. Boyer, H. Lardy, K. Myrbäck. Academic Press, New York 1963; 7: 25–83
  • Vallee B.L., Hoch F.L. Yeast alcohol dehydrogenase, a zinc metalloenzyme. Journal of the American Chemical Society 1955a; 77: 821–822
  • Vallee B.L., Hoch F.L. Zinc, a component of yeast alcohol dehydrogenase. Proceedings of the National Academy of Sciences, U.S.A. 1955b; 41: 327–338
  • Wallenfels K., Sund H. Mechanism of hydrogen transfer with pyridine nucleotides. I. Free SH-groups and the activity of yeast alcohol hydydrogenase. Biochemische Zeitschrift 1957; 329: 17–30
  • Woenckhaus M., Zoltobrocki J., Berghauser J., Jeck R. Specific incorporation of the coenzyme analogue 3-(3-bromacetylpyridine) propyladenosine pyrophosphate into the alcohol dehydrogenase from yeast. Hoppe Seylers Zeitschrift für Physiologische Chemie 1973; 354: 60–66

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