Control of Oxidative Damage in Rheumatoid Arthritis By Gold(I)-Thiolate Drugs

References

• Brown D. H., Smith W. E. The chemistry of the gold drugs used in the treatment of rheumatoid arthritis. Chemical Society Review 1980; 9: 217
   Web of Science ®Google Scholar
• Grootveld M. C., Razi M. T., Sadler P. J. Progress in the characterization of gold drugs. Clinical Rheumatology 1984; 351: 5
   Google Scholar
• Shaw C. F., III. The mammalian biochemistry of gold: an inorganic perspective of chrysotherapy. Inorganic Perspectives in Biology and Medicine 1979; 2: 287
   Web of Science ®Google Scholar
• Sadler P. J. The comparative evaluation of the physical and chemical properties of gold compounds. Journal of Rheumalholgy 1982; 58: 71
   Google Scholar
• Grootveld M. Studies of the reaction mechanisms of metal complexes of biological and immunochemical interest. PhD thesis, University of London. 1985
   Google Scholar
• Grootveld M., Sadler P. J. Difference between the structure of the anti-arthritic gold drug ‘Myocrisin’ in the solid state and in solution: a kinetic study of dissolution. Journal of Inorganic Biochemistry 1983; 19: 51
   Google Scholar
• Danpure C. J. Interaction of aurothiomalate with human serum albumin in vitro. Biochemical Society Transactions 1976; 4: 161
   Google Scholar
• Rayner M. H., Grootveld M., Sadler P. J. Molecular distribution of gold(I) in human blood plasma after treatment with the anti-arthritic drug disodium aurothiomalate. Clinical Pharmacology Research 1989, in press
   Google Scholar
• Danpure C. J., Fyfe D. A., Gumpel J. M. Distribution of gold among plasma fractions in rheumatoid patients undergoing chrysotherapy compared with its distribution in plasma incubated with aurothiomalate in vitro. Annals of the Rheumatic Diseases 1979; 38: 364
   Google Scholar
• Shaw C. F., III, Schmitz G., Thompson H. O., Witkeiwicz P. Bis(L-cysteinato)gold(I): chemical characterisation and identification in renal cortex cytoplasm. Journal of Inorganic Biochemistry 1974; 10: 317
   Google Scholar
• Ghadially F. N., Oryschak A. F., Mitchell D. M. Ultrastructural changes produced in rheumatoid synovial membrane by chrysotherapy. Annals of the Rheumatic Diseases 1976; 35: 67
   PubMed Web of Science ®Google Scholar
• Vernon-Roberts B., Dore J. L., Jessop J. D., Henderson W. J. Selective concentration and localisation of gold in macrophages of synovial and other tissues during and after chrysotherapy in rheumatoid pateints. Annals of the Rheumatic Diseases 1976; 35: 477
   PubMed Web of Science ®Google Scholar
• Graham G. G., Haavisto T. M., McNaught P. J., Browne C. D., Champion C. D. The effect of smoking on the distribution of gold in blood. Journal of Rheumatology 1982; 9(4): 527
   Google Scholar
• Graham G. G., Haavisto T. M., Jones H. M., Champion C. D. The effect of cyanide on the uptake of gold by red blood cells. Biochemical Pharmacology 1984; 33: 1257
   PubMed Web of Science ®Google Scholar
• Graham G. G., Bales J. R., Grootveld M. C., Sadler P. J. 1H, 13C NMR, and electronic absorption spectroscopic studies of the interaction of cyanide with aurothiomalate. Journal of Inorganic Biochemistry 1985; 23
   Google Scholar
• Gerber D. A. Inhibition of denaturation of human gamma globulin by a mixture of L-histidine, L-cysteine, and copper, and its clinical implication in rheumatoid arthritis. Arthritis and Rheumatism 1976; 19: 593
   Google Scholar
• Gerber D. A. Effect of gold thiomalate on protein denaturation. Journal of Pharmacology and Experimental Therapeutics 1964; 143: 137
   Google Scholar
• Persellin P. H., Ziff M. The effets of gold salts on lysosomal enzymes of peritoneal macrophage. Arthritis and Rheumatism 1966; 9: 57
   PubMed Web of Science ®Google Scholar
• Ennis R. S., Granda J. L., Posner A. S. Effects of gold salts and other drugs on the release and activity of lysosomal hydrolases. Arthritis and Rheumatism 1968; 11: 756
   PubMedGoogle Scholar
• Burkhardt D., Stephens R. W., Ghosh P., Taylor T. K.F. Inhibition of synovial fluid lysosomal glycosidases by antiarthritic gold preparations. Agents and Actions 1978; 8: 251
   PubMedGoogle Scholar
• Penneys N. S., Ziboh V., Gottlieb N. L., Katz S. Inhibition of prostaglandin syntheis and human epidermal growth enzymes by aurothiomalate in vitro: possible actions of gold in pemphigus. Journal of Investigative Dermatology 1974; 63: 356
   PubMedGoogle Scholar
• Stone K. J., Mather S. J., Gibson P. P. Selective inhibition of prostaglandin synthesis and biosynthesis by gold salts and phenylbutazone. Prostaglandins 1975; 10: 241
   Google Scholar
• Matsubara T., Ziff M. Inhibition of human endothelial cell proliferation by gold compounds. Journal of Clinical Investigation 1987; 79: 1490
   Google Scholar
• Rohozkova D., Steven F. S. Gold-containing drugs and the control of proteolytic enzymes. British Journal of Pharmacology 1983; 79: 181
   Google Scholar
• Nathan I., Finkelstein A. E., Walz D. T., Dvilansky A. Studies on the effect of auranofin. a new anti-arthritic agent, on platelet aggregation. Inflammation 1978; 3(2): 117
   Google Scholar
• Mallya S. K., Van Wart H. E. Inhibition of human neutrophil collagenase by gold(I) salts used in chrysotherapy. Biochemical and Biophysical Research Communications 1987; 144: 101
   Google Scholar
• Vernon-Roberts B., Jessop J. D., Dove I. Effect of gold salts and prednisolone on inflammatory cells, II. Annals of the Rheumatic Diseases 1973; 32: 301
   Google Scholar
• Norn S. Influence of anti-rheumatic agents on the release of histamine from rat peritoneal mast cells after an antigen-antibody reaction. Acta Pharmacology and Toxicology 1985; 22: 369
   Google Scholar
• Schultz D. R., Volankis J. E., Arnold P. J., Gottlieb N. L., Sakai K., Stroud R. M. Inactivation of CI in rheumatoid synovial fluid, purified CI and CI esterase, by gold compounds. Clinical and Experimental Immunology 1974; 27: 395
   Google Scholar
• Burge J. J., Fearonand D. T., Austen K. F. Inhibition of the altervative pathway of complement by sodium thiomalate in vitro. Journal of Immunology 1968; 120: 162S
   Google Scholar
• Matheson N. R. The effect of anti-arthritic drugs and related compounds on the human neutrophil myeloperoxidase system. Biochemical and Biophysical Research Communications 1982; 108: 259
   PubMed Web of Science ®Google Scholar
• Walz D. T., Griwold D. E. Immunopharmacology of gold sodium thiomalate and auranofin (SK and F D-39162). Inflammation 1978; 3: 117
   PubMedGoogle Scholar
• Adam M., Fretzek P., Kuhn K. Investigations on the reaction of metals with collagen in vitro. I. Comparison of the reaction of gold thiosulphate with collagen in vivo and in vitro. European Journal of Biochemistry 1986; 3: 407
   Google Scholar
• Adam M., Fretzek P., Kuhn K. Investigations of the reaction of metals with collagen in vivo II. The formation of crosslinks in the collagen of lathyritic rats after gold treatment in vivo. European Journal of Biochemistry 1986; 3: 441
   Google Scholar
• Gerber D. A. Inhibition of heat aggregation of human gamma globulin by histidine, gold thiomalate and penicillamine. Arthritis and Rheumatism 1971; 14A: 383
   Google Scholar
• Lorber A., Bouy R. A., Chang C. C. Relationship between serum gold content and distribution to serum immunoglobulins and complement. Nature and New Biology 1972; 69: 250
   Google Scholar
• Vernon-Roberts B. Action of gold salts on the inflammatory response and inflammatory cell function. Journal of Rheumalhology 1979; 5(suppl)120
   Google Scholar
• Gerber D. A. Possible role of a copper complex in the pathogenesis of rheumatoid arthritis. Trace Elements in the Pathogenesis Treatment of Inflammation, K. D. Rainsford, K. Bruneand, M. W. Whitehouse. Birkhouser Verlag, Basel 1981; 165–184, Agents and Actions Suppl. vol. 8
   Google Scholar
• Gerber D. A., Kornbluth A., Weiss S. Presence of an endogenous inhibitor of protein denaturation in the ultrafiltrate of normal serum: subnormal levels in rheumatoid arthritis. Arthritis Clinical Research. 1980; 28: 3461
   Google Scholar
• Halliwell B., Gutteridge J. M.C. The importance of free radicals and catalytic metal ions in human diseases. Molecular Aspects of Medicine 1985; 8: 89
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J. M.C., Blake D. R. Metal ions and oxygen radical reactions in inflammatory joint disease. Philosophical Transactions of the Royal Society (London) 1985; 311: 650
   Google Scholar
• McCord J. M. Free radicals and inflammation: protection of synovial fluid by SOD. Science 1974; 184: 529
   Google Scholar
• Blake D. R., Merry P., Unsworth J., Kidd B., Outhwaite J. M., Ballard R., Morris C. J., Gray L., Lunec J. Hypoxic-reperfusion injury in the inflamed human joint. Lancet 1989; i: 289
   Web of Science ®Google Scholar
• Merry P., Grootveld M., Blake D. R. Hypoxic-reperfusion injury in the inflamed human joint. Lancent 1989; i: 1023
   Google Scholar
• Merry P., Winyard P. G., Morris C. J., Grootveld M., Blake D. R. Oxygen free radicals, inflammation and synovitis: the current status. Annals of I he Rheumatic Diseases 1989; 48: 864
   PubMed Web of Science ®Google Scholar
• Davis P., Johnson C., Miller C. L., et al. Effects of gold compounds on the function of phagocytic cells. II. Inhibition of superoxide radical generation by tripeptide-activated polymor-phonuclearleucocytes. Arthritis and Rheumatism 1983; 26: 82
   PubMed Web of Science ®Google Scholar
• Batelli M. G., Delia Corte E., Stirpe F. Xanthine oxidase type D (dehydrogenase) in the intestine and other organs of the rat. Biochemical Journal 1972; 126: 747
   PubMed Web of Science ®Google Scholar
• Delia Corte E., Stripe F. The regulation of rat live xanthine oxidase: involvement of thiol groups in the conversion of the enxyme activity from the dehydrogenase (type D) to the oxidase (type O) and purification of the enzyme. Biochemical Journal 1972; 126: 739
   PubMed Web of Science ®Google Scholar
• McCord J. M. Oxygen-derived free radicals in postischaemic tissue injury. New England Journal of Medicine 1985; 312: 159
   PubMed Web of Science ®Google Scholar
• Granger D. N., Sennett M., McElearney P., Taylor A. E. Effect of local arterial hypotension on cat intestial capillary permeability. Gastroenterology 1980; 79: 474
   PubMedGoogle Scholar
• Granger D. N., Rutili G., McCord J. M. Superoxide radicals in feline intestinal ischaemia. Gastroenterology 1981; 81: 22
   PubMed Web of Science ®Google Scholar
• Schlafer M., Kane P. F., Kirsch M. M. Superoxide dismutase plus catalase enhance the eflicay of hypothermic cardioplegia to protect the globally ischaemic heart. Journal of Thoracic and Cardiovascular Surgery 1982; 83: 830
   PubMed Web of Science ®Google Scholar
• Stewart J. R., Blackwell W. H., Crute S. L., et al. Prevention of myocardial ischaemia reperfusion injury with oxygen free radical scavengers. Surgical Forum 1982; 33: 317
   Google Scholar
• Grootveld M., Sadler P. J., Unplublished Results
   Google Scholar
• Minta J. O., Williams D. Interactions of antirheumatic drugs with the superoxide generating system of activated human polymorphonuclear leucocytes. Journal of Rheumatology 1986; 13(3): 489
   Google Scholar
• Wildfeuer A. Action of anti-rheumatic drugs on the function of human leucocytes. Drug Research 1983; 33: 780
   Google Scholar
• Roisman F. R., Walz D. T., Finkelstein A. E. Superoxide radical production by human leucocytes exposed to immune complexes: inhibitory action of gold compounds. Inflammation 1983; 7: 355
   PubMedGoogle Scholar
• Harth M., Keown P. A., Orange J. Cells with immunoregulatory function: the human macrophages and the effects of remittive drugs. Journal of Rheumatology Supplement 1983; 11: 76
   Google Scholar
• Dillard C. J., Tappel A. I. Interaction of gold containing antiarthritic drugs with selenium: inhibition of selenium-glutathione peroxidase and the catalytic oxidation-reduction functions. ‘Free radicals and arthritic diseases’, Topics in Aging Research in Europe, A. J.C. Swaak, J. F. Koster, 1986; 11: 83
   Google Scholar
• Schmitz G., Minkel D. T., Gingrich D., Shaw C. F., III. The binding of gold(I) to metallothionein. Journal of Inorganic Biochemistry 1980; 12: 293
   PubMed Web of Science ®Google Scholar
• Weser U., Gartner A., Armann H. J. Copper-thionein catabolism and the rise of serum copper levels during systemic inflammation. ‘Free radicals and arthritic diseases’ Topics in Aging Research in Europe, A. J.G. Swaak, J. F. Koster, 1986; 11: 59
   Google Scholar
• Hurst N. P., Bcssac B., Nuki G. Superoxide anion (Of) generation by blood monocytes (macrophages): stimulant effect of gold and penicillamine during treatment of RA patients. Annals of the Rheumatic Diseases 1982; 14(b): 632
   Google Scholar
• Muijsers A. O., Cuperus R. A., Wevwer R. A proposal for the action mechanism of anti-arthritic drugs containing thiol groups such as d-penicillamine: interference with leucocyte myeloperoxidase activity, involvement of superoxide and formation of compound III. ‘Free radicals and arthritic diseases’ Topics in Aging Resech in Europe, A. J.G. Swaak, F. Koster, 1986; 11: 191
   Google Scholar
• Simpson R. B. Association constants of methylmecury with sulphydryl and other bases. Journal of the American Chemical Society 1961; 83: 4711
   Web of Science ®Google Scholar
• Razi M. T., Otiko G., Sadler P. J. Ligand exchange reactions of gold drugs in model systems and in red cells. ‘Platinum, Gold, and other Metal Chemotherapeutic Agents: Chemistry and Biochemistry’, S. J. Lippard. ACS Syposium Series, 209, 1983; 371
   Google Scholar
• Lorber A., Pearson C. M., Meredith L., Gantz-Mandell. Serum suphydryl determinations and significance in connective tissue diseases. Annals of International Medicine. 1964; 61: 423
   PubMed Web of Science ®Google Scholar
• Hall N. D., Blake D. R., Bacon P. A. Scrum thiol levels in early synovitis. Journal of Rheumatology. 1982; 9: 593
   Google Scholar
• Banford J. C., Brown P. H., Hazelton R. A., et al. Altered thiol status in patients with rheumatoid arthritis. Rheumatology International 1982; 2: 107
   Google Scholar
• Koster J. F., Bicmond P., Swaak A. J.G. Intracellular and extracellular sulphydryl levels in rheumatoid arthritis. Annals of the Rheumatic Diseases 1986; 45: 44
   PubMed Web of Science ®Google Scholar
• Hall N. D., Gillan A. H. Effects of antirheumatic drugs on protein sulphydryl reactivity of human serum. Journal of Pharmacy and Pharmacology 1979; 31: 676
   PubMedGoogle Scholar
• Munthe E., Guldal G., Jellum E. The influence of d-penicillamine. aurothiomalate and other drugs on intracellular glutathione concentration. Modulation of Autoimmunity and Disease. Praager Publications. 1981, Chapter 20
   Google Scholar
• Ward J., Danpure C. J., Fyfe D. A. Determination of gold in plasma and plasma fractions by atomic absorption spectrometry and by neutron activation analysis. Clinica Chimica Acta 1977; 81: 87
   PubMedGoogle Scholar
• Danpure C. J., Fyfe D. A., Gumple J. M. Distribution of gold among plasma fractions in rheumatoid patients under gold chrysotherapy compared with its distribution in plasma incubated with aurothiomalate in vitro. Annals of the Rheumatic Disorders. 1979; 38: 364
   Google Scholar
• Isab A. A., Sadler P. J. A carbon-13 nuclear magnetic reasonace study of thiol-exchange reactions of gold(I) thiomalate (‘Myocrisin’) including applications to cysteine derivatives. Journal of the Chemical Society. Dalton Transactions. 1982; 135
   Google Scholar
• Baker M. S., Fcigan J., Lowther D. A. The mechanism of chondrocyte hydrogen peroxide damage. Depletion of intracellular ATP due to supression of glycolysis caused by oxidation of glyceraldehyde-3-phosphate dehydrogenase. Journal of Rheumatology. 1989; 16: 1
   Google Scholar
• Hyslop P. A., Hinshaw D. B., Halsey A., Schraufstatter L. U., Sauerheber R. D., Spragg R. G., Jackson J. H., Cochrane C. G. Mechanisms of oxidant-mediated cell injury. The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. Journal of Biological Chemistry. 1988; 263(4): 1665
   Google Scholar
• Grootveld M., Unpublished results
   Google Scholar
• Tengvall P., Lundstrom I., Sjoquist L., Elwing H., Bjursten L. M. Titanium-hydrogen peroxide interaction: model studies of the influence of the inflammatory response on titanium implants. Biomaterials 1989; 10: 166
   PubMed Web of Science ®Google Scholar
• Brown D. H., Smith W. E., Fox P., Sturrock R. D. The reactions of gold(O) with amino acids and significance of these reactions in the biochemistry of gold. Inorganicu Chimica Acta 1982; 67: 27
   Google Scholar
• Lewis G., Shaw C. F., III. Competition of thiols and cyanide for gold(I). Inorganic Chemistry 1986; 25: 58
   Web of Science ®Google Scholar
• Pal T., Anguly A. Determination of cyanide through its reaction with gelatin-stabilised gold sol in air. Analyst 1987; 122: 1327
   Google Scholar
• Stelmaszynska T., Zgliczynski J. M. ‘Cyanide in Biology’, B. Vennerland, E. E. Conn, C. J. Knowles, J. Westley. Academic Press, London 1981; 371–383
   Google Scholar
• Gunnarsson P. O., Pettersson G. Inhibition of horse-liver aclochol dehydrogenase by Pt(CN)42- and Au(CN)2−. European Journal of Biochemistry 1974; 43: 479
   Google Scholar
• Shaw C. F., III, Eldridge J., Cancro M. P. 13C nmr studies of aurothioglucose: ligand exchange and redox disproportionation reactions. Journal of Inorganic Biochemistry 1981; 14: 267
   Web of Science ®Google Scholar
• Johnson A., Puddephatt J. Mechanistic studies of reactions of benzenethiol with methyl derivatives of platinum) 1) and gold(I)and (III). Journal of the Chemical Society, Dalton Transactions 1975; 115
   Google Scholar
• Younes M., Weser U. Superoxide dismutase activity of copper penicillamine: possible involvement of Cu(I) stabilised sulphur radical. Biochemical and Biophysical Research Communications 1977; 78: 1247
   PubMed Web of Science ®Google Scholar
• Boiteux A. F., Doborta M., Taylor M. G. The effects of gold drugs on lipid peroxidation, in abstracts of posters presented at the clinical reasearch centre meeting. (December 16th–17th 1985, London) on ‘iron, copper, zinc and sulphur - involvement in disease and therapy’. Inorganic Biochemistry Discussion Group
   Google Scholar
• Hill D. T., Sutton B. M. (2,3,4,6-Tetra-O-acetyl-1-thio-β-D-glucopyransato-S) (triethylphosphine) gold, C20HMO9SPAu. Crystal Structure Communications 1980; 9: 679
   Web of Science ®Google Scholar
• Razi M. T., Sadler P. J., Hill D. T., Sutton B. M. Proton, carbon-13 and phosphorus-31 nuclear magnetic resonance studies of (2,3,4,6-tetra-O-acetyl-1-thio-β-D-glucopyranosato-S) (triethylphosphine gold (Auranofin). a novel anti-arthritic agent. Journal of the Chemical Society, Dalton Transactions 1983; 1331
   Google Scholar
• Malik N. A., Otiko G., Razi M. T., Sadler P. J. NMR studies on ligand exchange and redox reactions of auranofin in vitro and in red cells. Proceedings of the Symposium on the Bioninorganic Chemistry of Gold Co-ordination Compounds. Smith, Kline and French Laboratories, Philadelphia 1983; 47
   Google Scholar
• Tepperman K., Finer R., Donovan S. Intestinal uptake and metabolism of auranofin, a new oral gold-based antiarthritic drug. Science 1984; 225: 430
   PubMed Web of Science ®Google Scholar
• Hemple J., Mikuriya Y. Ligand exchange reactions of ‘Ridaura’. Proceedings of the Symposium on the Bioniorganic Chemistry of Gold Co-ordination Compounds. Smith, Kline and French Laboratories, Philadelphia 1983; 37
   Google Scholar
• Intoccia A. P., Flanagen T. L., Walz D. T., et al. Pharmaco-kinetics of auranofin in animals. Journal of Rheumatology 1982; 9 (Suppl. 8): 90
   Google Scholar
• Brown D. H., McKinlay G., Smith W. E. Electronic and circular dichroism spectra of gold(I) complexes having sulphur- and phosphorous-containing ligands. Journal of the Chemical Society, Dalton Transactions 1977; 1874
   Google Scholar
• Malik N. A., Otiko G., Sadler P. J. Control of intra- and extra-cellular sulphydryl-disulphide balance with gold phosphine drugs: P nuclear magnetic resonance studies of human blood. Journal of Inorganic Biochemistry 1980; 12: 317
   PubMed Web of Science ®Google Scholar
• Walz D. T., DiMartino M. J., Sutton B. M. Design and laboratory evaluation of gold compounds as anti-inflammatory agents. ‘Anti-inflammatroy agents.’, R. A. Scherrer, M. S. Whitehouse. Academic Press, New York 1974; Vol. 1: 217–244
   Google Scholar
• Sutton B. M., McGusty E., Walz D. T., DiMartino M. J. Oral gold, antiarthritic properties of alkylphosphine gold coordiantion complexes. Journal of Medicinal Chemistry 1972; 15: 1095
   PubMed Web of Science ®Google Scholar
• Manabe T., Goda K., Kimura T. Chemical reactivity of labile sulphur of iron-sulphur proteins. The reaction of triphenyl phosphine. Biochimica et Biophysica Acta 1976; 428: 312
   Google Scholar
• Grootveld M., Otiko G., Sadler P. J., Cammack R. Reactions of triethylphosphine gold(I) complexes with haem proteins: novel spin-state changes in cytochrome b562, myoglobin and haemoglobin. Journal of Inorganic Biochemistry 1986; 27: 1
   Google Scholar
• Wallace W. J., Houtchems R. A., Holt J. M., Caughey W. S. Biochemical and Clinical Aspects of Haemoglobin Abnormalities, W. S. Caughey. Academic Press. 1978; 475
   Google Scholar
• Corey E. J., Mehrotra M. M., Khan A. U. Antiarthritic gold compounds effectively quench electronically excited singlet oxygen. Science 1978; 236: 68
   Google Scholar
• Rudge S. R., Perret D., Kelley M. Failure of oral sodium thiomalate to act as an alternative to intra-muscular gold. Annals of the Rheumatic Diseasese 1988; 47: 224
   Google Scholar
• Evans P. J., Bomford A., Halliwell B. Non-caerulopasmin copper and ferroxidase activity in mammalian serum Phenanthroline-delectable copper in human serum in Wilsons disease. Free Radical Research Communications 1989; 7: 55–62
   PubMed Web of Science ®Google Scholar
• Piper H. M. Energy deficiency, calcium overload or oxidative stress: Possible causes of irreversible ischaemic myocardial injury. Klinische Wochenschrift, 67: 465
   Google Scholar
• Joester K. E., Jung G., Weber U., Weser U. Superoxide dismutase activity of Cu2+ -amino acid chelates. FEBS Letters 1972; 25
   Google Scholar
• Wasil M., Halliwell B., Moorhouse C. P., Hutchinson D. C.S. Biologically-significant scavenging of the myeloperoxidase-derived oxidant hypocholorous acid by some anti-inflammatory drugs. Biochemical Pharmacology 1987; 26: 3847
   Google Scholar
• Ferrair R., Ceconi C., Curello S., Cargnoni A., Medici D. Oxygen free radicals and reperfusion injury: the effect of ischaemia and reperfusion on the cellular ability to neutralise oxygen toxicity. Journal of Molecular and Cellular Cardiology 1986; 18: 67
   Google Scholar
• Schäfer K., Bonifacic M., Bahnemann D., Asmus K. D. Addition of oxygen to organic sulphur radicals. The Journal of Physical Chemistry 1978; 82,26: 2777
   Google Scholar
• Lunec J., Brailsford S., Hewitt S. D., Morris C. J., Blake D. R. Free radicals: are they possible mediators of IgG denaturation and immune complex formation in RA?. ‘Free radicals and arthritic diseases’ Topics in Aging Research in Europe, A. J.C. Swaak, J. F. Koster, 1986; 11: 3
   Google Scholar
• Elder R. C., Eidness M. K., Heeg M. J., Tepperman K. G., Shaw C. F., III. Gold-based antiarthritic drugs and metabolites. ACS Symposium Series 1983; 209: 385
   Google Scholar
• Ghadially F. N. The techniques of electron probe X-ray analysis and the atomic composition of aurosomes. Journal of Rheumatology 1979; 6 (Suppl. 5): 25
   Google Scholar
• Hirsch J. C., Fedorko M. E., Cohn Z. A. vesicle fusion and formation at the surface of pinocytic vacuoles in macrophages. Journal of Cell Biology 1968; 38: 629
   PubMedGoogle Scholar
• Tamba M., Simone G., Quintiliani M. Interactions of thiyl free radicals with oxygen: a pulse radiolysis study. International Journal of Radii ion Biology 1986; 50: 595
   Web of Science ®Google Scholar
• Monig J., Asmus K. D., Forniand L. G., Willson R. L. On the reaction of molecular oxygen with thiyl radicals: a re-examination. International Journal of Radiation Biology 1987; 52: 589
   Web of Science ®Google Scholar
• Aruoma O. I., Halliwell B., Butler J., Hoey B. M. Apparent inactivation of α1antiproteinase by sulphur-containing radicals derived from penicillamine. Biochemical Pharmacology 1989; 38: 4353
   PubMed Web of Science ®Google Scholar
• Waud W. R., Rajagopalan K. V. Purification and properties of the NAD+ dependent (type D) and NAD+ independent (type O) forms of rat liver xanthine dehydrogenase. Archives of Biochemistry and Biophysics 1976; 172: 354
   PubMed Web of Science ®Google Scholar