PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2003 | 08 | 3 |

Tytuł artykułu

The rate constants of the reaction of hydroxyl radicals [OH] with alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The rate constants of the reactions of alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase with hydroxyl radicals were determined using the method of steady-state competitive reactions. Ethanol was used as a scavenger of hydroxyl radicals. The rate constants of the reactions of hydroxyl radicals with alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase were found to be 2.8·1012dm3mol-1s-1, and 1.6·1012dm3mol-1s-1, respectively.

Wydawca

-

Rocznik

Tom

08

Numer

3

Opis fizyczny

p.841-848,fig.

Twórcy

autor
  • University of Lodz, 90-237 Lodz, Banacha 12-16, Poland
autor

Bibliografia

  • 1.Buxton, G.V., Greenstock, C. L., Helman, W.P. and Ross, A.B. Critical review of rate constants for reactions of hydrated electrons. Hydrogen atoms and hydroxyl radicals (°OH/°O-) in aqueous solution. J. Phys.Chem. Ref. Data 17 (1988) 513-886.
  • 2.Sanner, T. and Pihl, A. Identification of the water radicals in X-ray inactivation of enzymes in solution and determination of their rate of interaction with the enzyme. Bioch. Biophys. Acta, 146 (1967) 298-301.
  • 3.Hummel, A. Kinetics in radiation chemistry, in: Radiation Chemistry: Principles and Applications., VCH Publisher, Inc., 1987, 97-136.
  • 4.Bonnichsen, R.K. and Brink, N.G. in: Methods in Enzymology (Colowick, S.P. and Kaplan, N.O. Eds), Liver Alcohol Dehydrogenase 1 (1955) 495-496.
  • 5.Amelunxen, R.E. and Carr, D.O. The crystallization and properties of glyceraldehyde-3-phosphate dehydrogenase isolated from rabbit muscle by a simplified procedure. Biochim. Biophys. Acta 132 (1967) 256.
  • 6.Von Sonntag, C. The chemical basis of radiation biology. In: Enzymes London-New York-Philadelphia, Taylor & Francis Ltd., 1987, 429-457.
  • 7.Klapper, M.H. and Faraggi, M. Application of pulse radiolysis to protein chemistry. Q. Rev. Biophys. 12 (1979) 465-519.
  • 8.Schuessler, H. and Herget, A. Oxygen effect in the radiolysis of proteins. I. Lactate dehydrogenase. Int. J. Radiat. Biol. 37 (1980) 71-80.
  • 9.Puchała, M. and Schuessler, H. Oxygen effect in the radiolysis of proteins. III. Haemoglobin. Int. J. Radiat. Biol. 64 (1993) 149-156.
  • 10.Bielski, B.H.J., Cabelli, D.E. and Arudi, R.L. Reactivity of HO2/O2- radicals in aqueous solution. J. Phys. Chem. Data 14 (1985) 1041-1100.
  • 11.Obinger, C., Furtmüller, P.G., Burner, U., Jantschko, W. and Regelsberger, G. Two-electron reduction and one-electron oxidation of organic hydroperoxides by human myeloperoxidase. FEBS Lett. 484 (2000) 139-143.
  • 12.Hayon, E., Ibata, T., Lichtin, N.N. and Simic, M. Sites of attack of hydroxyl radicals on amides in aqueous solution. II. The effect of branching to carbonyl and to nitrogen. J. Am. Chem. Soc. 93 (1971) 5388-5394.
  • 13.Schuessler, H. Navaratnam, S. and Distel, L. Pulse radiolysis on histones and serum albumin under different ionic conditions. Rad. Phys. Chem. 61 (2001) 123-128.
  • 14.Santiar, D., Ribiere, C., Nordman R. and Houee-Levin, C. Inactivation of Cu, Zn-superoxide dismutase by free radicals derived from ethanol metabolism: A γ radiolysis study. Free Rad. Biol. Med. 19 (1995) 121-127.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-5695ddd1-89c7-469d-adc1-d2ff24e73db4
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.