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- AZARI P. R., FEENEY R. E. Resistance of metal complexes of conalbumin and transferrin to proteolysis and to thermal denaturation. J Biol Chem. 1958 May;232(1):293–302. [PubMed] [Google Scholar]
- Aruoma O. I., Halliwell B. Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl-radical generation? Biochem J. 1987 Jan 1;241(1):273–278. doi: 10.1042/bj2410273. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baldwin D. A., Jenny E. R., Aisen P. The effect of human serum transferrin and milk lactoferrin on hydroxyl radical formation from superoxide and hydrogen peroxide. J Biol Chem. 1984 Nov 10;259(21):13391–13394. [PubMed] [Google Scholar]
- Calabrese L., Carbonaro M. An e.p.r. study of the non-equivalence of the copper sites of caeruloplasmin. Biochem J. 1986 Aug 15;238(1):291–295. doi: 10.1042/bj2380291. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gutteridge J. M. Antioxidant properties of the proteins caeruloplasmin, albumin and transferrin. A study of their activity in serum and synovial fluid from patients with rheumatoid arthritis. Biochim Biophys Acta. 1986 Jan 30;869(2):119–127. doi: 10.1016/0167-4838(86)90286-4. [DOI] [PubMed] [Google Scholar]
- Gutteridge J. M. Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Lett. 1986 Jun 9;201(2):291–295. doi: 10.1016/0014-5793(86)80626-3. [DOI] [PubMed] [Google Scholar]
- Gutteridge J. M., Paterson S. K., Segal A. W., Halliwell B. Inhibition of lipid peroxidation by the iron-binding protein lactoferrin. Biochem J. 1981 Oct 1;199(1):259–261. doi: 10.1042/bj1990259. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gutteridge J. M., Stocks J. Caeruloplasmin: physiological and pathological perspectives. Crit Rev Clin Lab Sci. 1981;14(4):257–329. doi: 10.3109/10408368109105866. [DOI] [PubMed] [Google Scholar]
- Halliwell B., Gutteridge J. M., Blake D. Metal ions and oxygen radical reactions in human inflammatory joint disease. Philos Trans R Soc Lond B Biol Sci. 1985 Dec 17;311(1152):659–671. doi: 10.1098/rstb.1985.0171. [DOI] [PubMed] [Google Scholar]
- Halliwell B., Gutteridge J. M. Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch Biochem Biophys. 1986 May 1;246(2):501–514. doi: 10.1016/0003-9861(86)90305-x. [DOI] [PubMed] [Google Scholar]
- Williams J. The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis. Biochem J. 1974 Sep;141(3):745–752. doi: 10.1042/bj1410745. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Winterbourn C. C. Lactoferrin-catalysed hydroxyl radical production. Additional requirement for a chelating agent. Biochem J. 1983 Jan 15;210(1):15–19. doi: 10.1042/bj2100015. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Winterbourn C. C., Molloy A. L. Susceptibilities of lactoferrin and transferrin to myeloperoxidase-dependent loss of iron-binding capacity. Biochem J. 1988 Mar 1;250(2):613–616. doi: 10.1042/bj2500613. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Winyard P., Lunec J., Brailsford S., Blake D. Action of free radical generating systems upon the biological and immunological properties of caeruloplasmin. Int J Biochem. 1984;16(12):1273–1278. doi: 10.1016/0020-711x(84)90227-1. [DOI] [PubMed] [Google Scholar]