References
- Taube H. Mechanisms of oxidation with oxygen. J Gen Physiol 1965; 49: 29–52.
- van Heyningen R, Pirie A. The metabolism of naphthalene and its toxic effect on the eye. Biochem J 1967; 102: 842–852.
- Zigman S, Griess G, Yulo T et al. Ocular protein alterations by near UV light. Exp Eye Res 1973; 15: 255–264.
- Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979; 59: 526–605.
- Giblin F J, Chakrapani B, Reddy V N. The effect of X-irradiation on lens reducing systems. Invest Ophthalmol Vis Sci 1979; 18: 468–475.
- Zigman S. In: Duncan G, ed. Mechanisms of Cataract Formation in the Human Lens. London: Academic Press, 1981: pp 117–149.
- Iwata S, Maesato T. Studies on the mercapturic acid pathway in the rabbit lens. Exp Eye Res 1988; 47: 479–488.
- Harding J J. Free and protein-bound glutathione in normal and cataractous human lenses. Biochem J 1970; 117: 957–960.
- Truscott R J W, Augusteyn R C. Oxidative changes in human lens proteins during senile cataract formation. Biochim Biophys Acta 1977; 492: 43–52.
- Truscott R J W, Augusteyn R C. The state of sulfhydryl groups in normal and cataractous human lenses. Exp Eye Res 1977; 25: 139–148.
- Augusteyn R C. In: Duncan G, ed. Mechanisms of Cataract Formation in the Human Lens. London: Academic Press, 1981; pp 71–115.
- Harding J J, Crabbe M J. In: Davson H, ed. The Eye, vol. IB. London: Academic Press, 1984; pp 207.
- Sato S. Aldose reductase the major protein associated with naphthalene dihydrodiol dehydrogenase activity in rat lens. Invest Ophthalmol Vis Sci 1993; 34: 3172–3178.
- Hara A, Harada T, Nakagawa M et al. Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase. Biochem J 1989; 264: 403–407.
- Kimura S, Takehana M, and Iwata S. Scavenging system in crystalline lens: activity of GSH transferase. Third National Congress of Eye Research: Japanese Chapter of International Society for Eye Research. 1981; 44.
- Ahmad H, Singh S V, Medh R D et al. Differential expression of α, μ and π classes of isozymes of glutathione S-transferase in bovine lens, cornea, and retina. Arch Biochem Biophys 1988; 266: 416–426.
- Nishinaka T, Terada T, Nanjo H et al. Difference in glutathione S-transferase response to oxidative stress between porcine and bovine lens. Exp Eye Res 1993; 56: 299–303.
- Nishinaka T, Yasunari C, Abe A et al. Differential expression of three classes of glutathione S-transferase (GST) isozymes in the lens among animal species: Purification of GST isozymes in rabbit lens. Curr Eye Res 1993; 12: 333–340.
- Mannervik B, Awasthi Y C, Board P G et al. Nomenclature for human glutathione S-transferases. Biochem J 1992; 282: 305–306.
- Jakoby W B, Habig W H. Glutathione transferase. In: Jakoby W B, ed. Enzymology Basis of Detoxication, Vol. 2. 1980: pp. 63–94.
- Litwack G, Ketterer B, Arisas I M. Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogen and a number of exogeneous organic anions. Nature 1977; 234: 466–467.
- Prohaska J R, Ganther H E. Glutathione peroxidase activity of glutathione-S-transferases purified from rat liver. Biochem Biophys Res Commun 1977; 76: 437–445.
- Awasthi Y C, Dao D D, Saneto R P. Interrelationship between anionic and cationic forms of glutathione S-transferases of human liver. Biochem J 1980; 191: 1–10.
- Rathbun W B, Hanson S K. Glutathione metabolic pathway as a scavenging system in the lens. Ophthalmic Res 1979; 11: 172–176.
- Nishinaka T, Fujioka M, Nanjo H et al. Pig lens glutathione S-transferase belongs to class Pi enzyme. Biochem Biophys Res Commun 1991; 176: 966–971.
- Nishinaka T, Kodaka R, Nanjo H et al. Purification and characterization of glutathione S-transferase isozymes in dog lens. Int J Biochem 1992; 24: 1737–1742.
- Nishinaka T, Kodaka R, Nanjo H et al. Glutathione S-transferase isozymes in rat lens. Biochem Int 1992; 26: 135–141.
- Iwata S. In: Iwata S, ed. Suishotai (in Japanese). Tokyo: Medical Aoi Shuppan, 1986: 351–354.
- Terada T, Maeda H, Okamoto K et al. Modulation of glutathione S-transferase activity by a thiol/disulfide exchange reaction and involvement of thiol/transferase. Arch Biochem Biophys 1993; 300: 495–500.
- Habig W H, Jakoby W B. Assays for differentiation of glutathione S-transferases. Methods Enzymol. 1981; 77: 398–405.
- Shen H, Tsuchida S, Tamai K et al. Identification of cysteine residues involved in disulfide formation in the inactivation of glutathione transferase P-form by hydrogen peroxide. Arch Biochem Biophys 1993; 300: 137–141.