References
- Baumer R. Beitrag zur rechnergestützten quantitativen Proteinbestimmung nach gelelektrophoretischer Auftrennung. 1988, Thesis Universität Erlangen-Nürnberg.
- Böhlen P., Stein S., Dairman W., Udenfriend S. Fluorometric assay of proteins in the nanogram range. Archives of Biochemistry and Biophysics 1973; 155: 213–220
- Davies K.J.A. Protein damage and degradation by oxygen radicals I. General aspects. Journal of Biological Chemistry 1987; 262: 9895–9901
- Davies K.J.A, Delsignore M.E. Protein damage and degradation by oxygen radicals III. Modification of secondary and tertiary structure. Journal of Biological Chemistry 1987; 262: 9908–9913
- Drabkin D.L. The crystallographic and optical properties of the hemoglobin of man. Journal of Biological Chemistry 1946; 164: 703–723
- Fermi G., Perutz M.F. Haemoglobin and myoglobin. Atlas of Molecular Structures in Biology, D.C. Phillips, F.M. Richards. Clarendon, Oxford 1981, In
- Garrison W.M. Reaction mechanisms in the radiolysis of peptides, polypeptides and proteins. Chemical Reviews 1987; 87: 381–398
- King N.K., Winfield M.E. The mechanism of metmyoglobin oxidation. Journal of Biological Chemistry 1963; 238: 1520–1528
- Klapper M.H., Faraggi M. Applications of pulse radiolysis to protein chemistry. Quaterly Reviews of Biophysics 1979; 12: 465–546
- Makada H.A., Garrison W.M. Radiolytic oxidation of peptide derivates of glycine in aqueous solution. Radiation Research 1972; 50: 48–55
- Ortiz de Montellano P.R. Control of the catalytic activity of prosthetic heme by the structure of hemoproteins. Accounts of Chemical Research 1987; 20: 289–294
- Schuessler H., Freundl K. Reactions of formate and ethanol radicals with bovine serum albumin studied by electrophoresis. International Journal of Radiation Biology 1983; 44: 17–29
- Schuessler H., Herget A. Oxygen effect in the radiolysis of proteins. I. Lactate dehydrogenase. International Journal of Radiation Biology 1980; 37: 71–80
- 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
- Szweda-Lewandowska Z., Puchala M., Osmulski P.A., Rosin J. Radiation-induced changes of structural and functional properties of human hemoglobin. II. Structural and functional characterization of irradiated deoxyhemoglobin. Radiation and Environmental Biophysics 1989; 28: 47–58
- Udenfriend S., Stein S., Böhlen P., Dairman W. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 1972; 178: 871–872
- von Sonntag C. The Chemical Basis of Radiation Biology. Taylor & Francis, London 1987; 33–33
- Weber K., Osborn M. Proteins and sodium dodecyl sulfate: molecular weight determination on polyacrylamide gels and related precedures. The Proteins3rd Edn, H. Neurath, R.L. Hill. Academic, New York, London 1975; 1: 179–223, In
- Whitburn K.D. Interaction of oxymyoglobin with hydrogenperoxide: the formation of ferrylmyoglobin at moderate excesses of hydrogen peroxide. Archives of Biochemistry and Biophysics 1987; 253: 419–430
- Whitburn K.D., Hoffmann M.Z. Interaction of radiation generated-radicals with myoglobin in aqueous solution III. Effects of oxygen and catalase on the product distribution in solutions of ferrimyoglobin containing N2O. International Journal of Radiation Biology 1985; 47: 167–179
- Whitburn K.D., Hoffmann M.Z., Taub J.A. Interaction of radiation generated-radicals with myoglobin in aqueous solution-II. Analysis of product yields for hydroxyl radicals with oxymyoglobin under deaerated conditions. Radiation Physical Chemistry 1984; 23: 271–278
- Wolff S.P., Garner A., Dean R.T. Free radicals, lipids and protein degradation. Trends in Biochemical Science 1986; 11: 27–31
- Young L.J., Canghey W.S. Autoreduction phenomena of bovine heart cytochrome c oxidase and other metalloproteins. Journal of Biological Chemistry 1987; 262: 15019–15025