Ames, B. N., Shigenaga, M. K. & Hagen, T. M. (1993). Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. USA 90: 7915-7922.
Baruchel, S, Viav, G., Olivier. R., Bounous, G., Wainberg, M. (1996). Nutraceutical modulation of GSH with a humanized native milk serum protein isolate, Immunocal: Application AIDS and cancer is oxidative stress and redox regulation: Cellular signaling, AIDS, cancer and other diseases. Symposium, Institute Pasteur
Bjorck, L., Rosen, C., Marshall, V., and Reiter B. (1975). Antibacterial Activity of the Lactoperoxidase System in Milk Against Pseudomonads and Other Gram-Negative Bacteria, Appl. Microbiol., 30, 199.
Bounous, G., and P. Gold. (1991). The biological activity of un-denatured whey proteins: role of glutathione. Clin. Invest Med.; 14:296-309
DeLeve LD, Kaplowitz N. (1991). Glutathione metabolism and its role in hepatotoxicity. Pharmacol Ther Dec; 52(3):287-305. Review.
Droege, W., E. Holm. (1997). Role of Cysteine and glutathione in HIV infection and other diseases associated with muscle wasting and immunological dysfunction. [Review] [91 refs.]. FASEBJ 1997, 11:1077-1089.
Droege, W., HP Eck, S. Mihm, D. Galter. (1994). Abnormal redox regulations in HIV infection and other immunodeficiency diseases. In: Oxidative Stress, cell activation and viral infection. C. Pasquier et al. (eds..). Birkauser Verlag, Basel, Switzerland, 285
Gutman, J. Schettini, S. (1998). The ultimate GSH handbook. Montreal: Gutman and Schettini Enr.
Harmsen, M.C., et al. (1995). Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. J. Infec. Dis. 172, 380-388.
Kawakami, H. et al. (1993). Effect of lactoferrin on iron solubility under neutral conditions. Biosci. Biotech. Biochem. 57(8), 1376-1377.
Kawasaki et al. (1993). Inhibition of kappa-casein glycomacropeptide and lactoferrin of influenza virus hemagglutination. Biosci Biotech Biochem 57 (7), 1214-1215.
Lomaestro BM, Malone M. (1995). Glutathione in health and disease: pharmacotherapeutic issues. Annals Pharmacotherapy; 29:1263-73
Marchetti et al. (1998). Metal complexes of bovine lactoferrin inhibit in vitro replication of Herpes simplex virus type 1 and 2. BioMetals 11, 89-94.
Marx, J.J.M., and van Asbeck, B.S. (1996). Use of iron chelators in preventing hydroxyl radical damage: Adult Respiratory Distress Syndrome as an experimental model for the pathophysiology and treatment of oxygen-radical-mediated tissue damage. Acta Hematology. 95, 49-62.
Meister, A. (1984). New aspects of glutathione biochemistry and transport selective alteration of glutathione metabolism. Nutr Rev 42: 397-410
Meister, A. (1994). The antioxidant effects of glutathione ascorbic acid. In: Oxidative stress, Cell Activation and Viral Infection. C. Pasquier et al. (eds..) Birkauser Verlag Basel, Switzerland 101-111
Noelle, RJ, DA Lawrence. (1981). Determination of glutathione in lymphocytes and possible association of redox state and proliferative capacity of lymphocytes. Biochem. J. 198:571-579
Reiter, B. (1985). The biological significance of the non-immunoglobulin protective proteins in milk. Developments in Dairy Chemistry, 3, 281-336.
Renner, E. (Ed.), (1989). Micronutrients in milk and milk-based food products. 1-70, 134-138, 275-276.
Samaranayake et al. (1997). The antifungal effect of lactoferrin and lysozyme on Candida krusei and Candida albicans, APMIS 105, 875-883.
Sanchez L., Calvo M., Brock, J.H. (1992). TMBiological role of lactoferrinTM, Archives of Disease in Childhood, 67, 657-661.
Superti et al. (1997). Antirotaviral activity of milk proteins: lactoferrin prevents rotavirus infection in the enterocyte-like cell line HT-29, Med Microbiol Immunol 186, 83-91.
Yamauchi, K. Biologically functional proteins of milk and peptides derived from milk proteins, 75th Annual Session of the IDF, Tokyo, Oct. 1991.
Yi, M. et al. (1997). Hepatitis C virus envelope proteins bind lactoferrin. J. Virol. 71 (8), 5997-6002. |