REFERENCES
- Stryer L. Biochemistry. 3rd ed. 1988. W. H. Freeman, New York 1090
- Reddy V N. Metabolism of glutathione in the lens. Exp Eye Res. 1971; 11: 310–328, [PUBMED], [INFOTRIEVE], [CSA]
- Reddy V N. Glutathione and its function in the lens—an overview. Exp Eye Res. 1990; 50: 771–778, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Giblin F J. Glutathione: a vital lens antioxidant. J Ocular Pharmacol Therapeutics. 2000; 16: 121–135, [CSA]
- Lou M F. Redox regulation in the lens. Prog Retinal Eye Res. 2003; 22: 657–682, [CSA], [CROSSREF]
- Harding J J. Free and protein-bound glutathione in normal and cataractous human lenses. Bioche J. 1970; 117: 957–960, [CSA]
- Harding J J, Blakytny R, Ganea E. Glutathione in disease. Biochem Soc Trans. 1996; 24: 881–884, [PUBMED], [INFOTRIEVE], [CSA]
- Harding J J. Affinity chromatography in the purification of glutathione reductase. J. Chromatogr. 1973; 77: 191–199, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Rogers K M, Augusteyn R C. Glutathione reductase in normal and cataractous human lenses. Exp. Eye Res. 1978; 27: 719–721, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Rao G N, Sadasivudu B, Cotlier E. Studies on glutathione S-transferase, glutathione peroxidase and glutathione reductase in human normal and cataractous lenses. Ophthalmic Res. 1983; 15: 173–179, [PUBMED], [INFOTRIEVE], [CSA]
- Friedburg D, Manthey K F. Glutathione and NADP linked enzymes in human senile cataract. Exp Eye Res. 1973; 15: 173–177, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Babizhayev M A, Deyev A I, Chernikov A V. Peroxide-metabolizing systems of the crystalline lens. Biochim Biophy Acta. 1992; 1138: 11–19, [CSA]
- Xie P Y, Kanai A, Nakajima A, Kitahara S, Ohtsu A, Fujii K. Glutathione and glutathione-related enzymes in human cataractous lenses. Ophthalmic Res. 1991; 23: 133–140, [PUBMED], [INFOTRIEVE], [CSA]
- Ohrloff C, Hockwin O, Olson R, Dickman S. Glutathione peroxidase, glutathione reductase and superoxide dismutase in the aging lens. Curr. Eye Res. 1984; 3: 109–115, [PUBMED], [INFOTRIEVE], [CSA]
- Srivastava S K, Villacorte D, Arya D V. Letter: Distribution of glutathione reductase in lens epithelium, cortex and nucleus in various species and in human cataractous lenses. Exp Eye Res. 1973; 16: 519–521, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Harding J J. Cataract, biochemistry, epidemiology and pharmacology. 1st ed. 1991. Chapman & Hall, London 2003
- Harding J J. Can drugs or micronutrients prevent cataract?. Drugs and Aging 2001; 18: 473–486, [PUBMED], [INFOTRIEVE], [CSA]
- Porras P, Pedrajas J R, Martinez-Galisteo E, Padilla C A, Johansson C, Holmgren A, Barcena J A. Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency. Bioche Biophy Res Commun. 2002; 295: 1046–1051, [CSA], [CROSSREF]
- Raghavachari N, Lou M F. Evidence for the presence of thioltransferase in the lens. Exp Eye Res. 1996; 63: 433–441, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Xing K Y, Lou M F. Effect of H(2)O(2)on human lens epithelial cells and the possible mechanism for oxidative damage repair by thioltransferase. Exp Eye Res. 2002; 74: 113–122, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Xing K, Lou M F. The possible physiological function of thioltransferase in cells. FASEB J. 2003; 17: 2088–2090, [PUBMED], [INFOTRIEVE], [CSA]
- Netto L E, Stadtman E R. The iron-catalyzed oxidation of dithiothreitol is a biphasic process: hydrogen peroxide is involved in the initiation of a free radical chain of reactions. Arc Bio Biophys. 1996; 333: 233–242, [CSA], [CROSSREF]
- Bhuyan K C, Bhuyan D K, Santos O, Podos S M. Antioxidant and anticataractogenic effects of topical captopril in diquat-induced cataract in rabbits. Free Radi Bio Med. 1992; 12: 251–261, [CSA], [CROSSREF]
- Follansbee M H, Beyer K HJ, Vesell E S. Studies on pyrazinoylguanidine. 6. Prevention of cataracts in STZ-diabetic rats. Pharmacology. 1997; 54: 256–260, [PUBMED], [INFOTRIEVE], [CSA]
- Ellis R J. Breakthroughs and views, Do Molecular Chaperones Have to Be Proteins?. Bio Biophys Res Commun. 1997; 238: 687–692, [CSA], [CROSSREF]
- Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Nati Acad Sci USA. 1992; 89: 10449–10453, [CSA]
- Heath M M, Rixon K C, Harding J J. Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, alpha-crystallin. Bio Biophys Acta. 1996; 1315: 176–184, [CSA]
- Ganea E, Harding J J. Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. Eur J Bio. 1995; 231: 181–185, [CSA], [CROSSREF]
- Ganea E, Harding J J. Inhibition of 6-phosphogluconate dehydrogenase by carbamylation and protection by alpha-crystallin, a chaperone-like protein. Bio Biophys Res Commun. 1996; 222: 626–631, [CSA], [CROSSREF]
- Hook D W, Harding J J. Alpha-crystallin acting as a molecular chaperone protects catalase against steroid-induced inactivation. FEBS Letters. 1996; 382: 281–284, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Derham B K, Harding J J. Effect of aging on the chaperone-like function of human alpha-crystallin assessed by three methods. Bioc J. 1997; 328: 763–768, [CSA]
- Blakytny R, Harding J J. Bovine and human alpha-crystallins as molecular chaperones: prevention of the inactivation of glutathione reductase by fructation. Exp Eye Res. 1997; 64: 1051–1058, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Rachdan D, Lou M F, Harding J J. Revival of inactive glyceraldehyde 3-phosphate dehydrogenase in human cataract lenses by reduction. Exp Eye Res. 2004; 79: 105–109, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Pirie A. Color and solubility of the proteins of human cataracts. Invest Ophthalmol. 1968; 7: 634–650, [PUBMED], [INFOTRIEVE], [CSA]
- Qiao F, Xing K, Liu A, Ehlers N, Raghavachari N, Lou M F. Human lens thioltransferase: cloning, purification, and function. Invest Ophthalmol Visual Sci. 2001; 42: 743–751, [CSA]
- Slingsby C, Bateman O A. Rapid separation of bovine beta-crystallin subunits beta B1, beta B2, beta B3, beta A3 and beta A4. Exp Eye Res. 1990; 51: 21–26, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Laemmli U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227: 680–685, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Bergmeyer H U. Methods of Enzymatic Analysis. Verlag Chemie; Academic Press, Weinheim/Bergstr; New York 1963; 1064
- Ganea E, Harding J J. α -Crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase. Biochem J., 345: 467–472, [CSA], [CROSSREF]