Radical-Induced Damage to Bovine Serum Albumin: Role of the Cysteine Residue

References

• Halliwcll B., Gutteridge J. M.C. Free Radicals in Biology and Medicine, 2nd Ed. Clarendon Press, Oxford 1989
   Google Scholar
• Wolff S. P., Garner A., Dean R. T. Free radicals, lipids and protein degradation. Trends in Biochemical Science 1986; 11: 27–31
   Web of Science ®Google Scholar
• Wolff S. P., Dean R. T. Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis. Biochemical Journal 1986; 234: 399–403
   PubMed Web of Science ®Google Scholar
• Davies K. J.A. Protein damage and degradation by oxygen radicals. The Journal of Biological Chemistry 1987; 262: 9895–9901
   PubMed Web of Science ®Google Scholar
• Hunt J. V., Simpson J. A., Dean R. T. Hydroperoxide-medialed fragmentation of proteins. Biochemical Journal 1988; 250: 87–93
   PubMed Web of Science ®Google Scholar
• Davies K. J.A., Goldberg A. L. Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes. The Journal of Biological Chemistry 1987; 262: 8220–8226
   PubMed Web of Science ®Google Scholar
• Davies K. J.A., Goldberg A. L. Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells. The Journal of Biological Chemistry 1987; 262: 8227–8234
   PubMed Web of Science ®Google Scholar
• Grant A. J., Jessup W., Dean R. T. Accelerated endocytosis and incomplete catabolism of radical-damaged protein. Biochimica et Biophysica Acta 1992; 1134: 203–209
   PubMed Web of Science ®Google Scholar
• Schuessler H., Herget A. Oxygen effect in the radiolysis of proteins. I. Lactate dehydrogenase. International Journal of Radiation Biology 1980; 37: 71–80
   Web of Science ®Google Scholar
• Hajos G., Delcinee H. Structural investigation of radiation-induced aggregates of ribonuclease. International Journal of Radiation Biology 1983; 44: 333–342
   Web of Science ®Google Scholar
• Schuessler H., Freundle K. Reactions of formate and ethanol radicals with bovine serum albumin studied by electrophoresis. International Journal of Radiation Biology 1983; 44: 17–29
   Web of Science ®Google Scholar
• Schuessler H., Schilling K. Oxygen effect in the radiolysis of proteins. Part 2. Bovine serum albumin. International Journal of Radiation Biology 1984; 45: 267–281
   Web of Science ®Google Scholar
• Clement J. R., Armstrong D. A., Klasson N. V., Gillis H. A. Pulse radiolysis of aqueous papain. Canadian Journal of Chemistry 1972; 50: 2833–2840
   Web of Science ®Google Scholar
• Lin W. S., Clement J. R., Gaucher G. M., Armstrong D. A. Repairable and non-repairable inactivation of irradiated aqueous papain. Effects of hydroxyl, hyperoxide, hydrated electron, and hydrogen peroxide. Radiation Research 1975; 62: 438–455
   PubMed Web of Science ®Google Scholar
• Buchanan J. D., Armstrong D. A. The radiolysis of glyceraldehyde-3-phosphate dehydrogenase. International Journal of Radiation Biology 1978; 33: 409–418
   Web of Science ®Google Scholar
• Prutz W. A. Radiation Research, E. M. Fielden, J. F. Fowler, J. H. Hendry, D. Scott. Taylor and Francis, London 1987; 2: 134
   Google Scholar
• Prutz W. A. Free radical transfer involving sulphur peptide functions. Sulfur-Centered Reactive Intermediates in Chemistry and Biology, C. Chatgilialoglu, K.-D. Asmus. Plenum Press, New York 1990; 389–399
   Google Scholar
• Graceffa P. Spin labelling of protein sulfhydryl groups by spin trapping and a sulfur radical: application to bovine serum albumin and myosin. Archives of Biochemistry and Biophysics 1983; 225: 802–808
   PubMed Web of Science ®Google Scholar
• Davies M. J., Forni L. G., Shuter S. L. Electron spin resonance and pulse radiolysis studies on the spin trapping of sulphur-centred radicals. Chemico-Biological Interactions 1987; 61: 177–188
   PubMed Web of Science ®Google Scholar
• Maples K. R., Kennedy C. H., Jordan S. J., Mason R. P. In vivo thiyl free radical formation from haemoglobin following administration of hydroperoxides. Archives of Biochemistry and Biophysics 1990; 277: 402–409
   PubMed Web of Science ®Google Scholar
• Davies M. J., Gilbert B. C., Haywood R. M. Radical-induced damage to proteins: E.S.R. spin-trapping studies. Free Radical Research Communications 1991; 15: 111–127
   PubMed Web of Science ®Google Scholar
• Means G. E., Feeney R. E. Chemical modification of proteins. Holden-Day Inc., San Francisco 1971
   Google Scholar
• Kaur H., Leung K. H.W., Perkins M. J. A water-soluble, nitroso-aromatic spin-trap. Journal of the Chemical Society, Chemical Communications 1981; 142–143
   Google Scholar
• Schneider D. J., Freed J. H. Spin-labelling theory and applications. Biological Magnetic Resonance, L. J. Berliner, J. Reuben. Plenum Press. 1989; 8: 68–72
   Google Scholar
• Wolf W., Kertesz J. C., Landgraf W. C. E.S.R studies of free radicals in solution. I. Oxidation of cysteine and related thiols with eerie ion. Journal of Magnetic Resonance 1969; 1: 618–632
   Google Scholar
• Buettner G. R. Spin trapping: E.s.r. parameters of spin adducts. Free Radical Biology and Medicine 1987; 3: 259–303
   PubMed Web of Science ®Google Scholar
• Stone T. J., Waters W. A. Aryloxy-radicals. Part 1. Electron spin resonance spectra of radicals from some substituted monohydric phenols. Journal of the Chemical Society 1964; 213–218
   Google Scholar
• Dixon W. T., Murphy D. The electron spin resonance spectra of alkyl aryl ether radical cations. Journal of the Chemical Society, Perkin Transactions 1976; 2: 1823–1828
   Google Scholar
• Buxton G. V., Greenstock C. L., Helman W. P., Ross A. B. Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals in aqueous solution. Journal of Physical and Chemical Reference Data 1988; 1: 513–886
   Google Scholar
• Taniguchi H. An electron spin resonance study of organosulfur radicals produced in electron-irradiated aqueous solutions. Spin trapping with nitromethane aci-anion and 2-methyl-2-nitrosopropane. The Journal of Physical Chemisity 1984; 88: 6245–6250
   Web of Science ®Google Scholar
• Schoneich C., Bonifacic M., Asmus K.-D. Reversible H-atom abstraction from alcohols by thiyl radicals-determination of absolute rate constants by pulse radiolysis. Free Radical Research Communications 1989; 6: 393–405
   PubMed Web of Science ®Google Scholar
• Schoneich C., Asmus K.-D., Dillinger U., von Bruckhausen F. Thiyl radical attack on polyunsaturated fatty-acids - a possible route to lipid peroxidation;. Biochemical and Biophysical Research Communications 1989; 161: 113–120
   PubMed Web of Science ®Google Scholar
• Schoneich C., Dillinger U., von Bruckhausen F., Asmus K.-D. Oxidation of polyunsaturated fatty acids and lipids through thiyl and sulfonyl radicals: reaction kinetics, and influence of oxygen and structure of thiyl radicals. Archives of Biochemistry and Biophysics 1992; 292: 456–467
   PubMed Web of Science ®Google Scholar