Comparison of purified lens glutathione S-transferase isozymes from rabbit with other species

References

• Mannervik B., Danielson U. H. Glutathione transferases—structure and catalytic activity. CRC Crit. Rev. Biochem. 1988; 23: 283–337
   PubMed Web of Science ®Google Scholar
• Boyer T. D. The glutathione S‐transferase: an update. Hepatology 1989; 9: 486–496
   PubMed Web of Science ®Google Scholar
• Pickett C. B., Lu A. Y.H. Glutathione S‐transferases: gene structure, regulation, and biological function. Annu. Rev. Biochem. 1989; 58: 743–764
   PubMed Web of Science ®Google Scholar
• Coles B., Ketterer B. The role of glutathione transferases in chemical carcinogenesis. CRC Crit. Rev. Biochem. Mol. Biol. 1990; 25: 47–70
   PubMed Web of Science ®Google Scholar
• Listowsky I., Abramovitz M., Homma H., Niitsu Y. Intracellular binding and transport of hormones and xenobiotics by glutathione‐S‐transferases. Drug Metab. Rev. 1988; 19: 305–318
   PubMed Web of Science ®Google Scholar
• Mannervik B., Ålin P., Guthenberg C., Jensson H., Tahir M. K., Warmholm M., Jörnvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 7202–7206
   PubMed Web of Science ®Google Scholar
• Rathbun W. B., Hanson S. K. Glutathione metabolic pathway as a scavenging system in the lens. Ophthalmic Res. 1979; 11: 172–176
   Web of Science ®Google Scholar
• Augusteyn R. C. Protein modification in cataract: possible oxidative mechanisms. Mechanisms of Cataract Formation in the Human Lens, G. Duncan. Academic Press, London 1981; 71–115
   Google Scholar
• Iwata S., Maesato T. Studies on the mercapturic acid pathway in the rabbit lens. Exp. Eye Res. 1988; 47: 479–488
   PubMed Web of Science ®Google Scholar
• Nishinaka T., Fujioka M., Nanjo H., Nishikawa J., Mizoguchi T., Terada T., Nishihara T. Pig lens glutathione S‐transferase belongs to class Pi enzyme. Biochem. Biophys. Res. Commun. 1991; 176: 966–971
   PubMed Web of Science ®Google Scholar
• Ahmad H., Singh S. V., Medh R. D., Ansari G. A.S., Kurosky A., Awasthi Y. C. 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
   PubMed Web of Science ®Google Scholar
• Nishinaka T., Kodaka R., Nanjo H., Terada T., Mizoguchi T., Nishihara T. Glutathione S‐transferase isozymes in rat lens. Biochem. Int. 1992; 26: 135–141
   PubMedGoogle Scholar
• Nishinaka T., Kodaka R., Nanjo H., Terada T., Mizoguchi T., Nishihara T. Purification and characterization of glutathione S‐transferase isozymes in dog lens. Int. J. Biochem. 1992; 24: 1737–1742
   PubMedGoogle Scholar
• Singh S. V., Srivastava S. K., Awasthi Y. C. Purification and characterization of the two forms of glutathione S‐transferase present in human lens. Exp. Eye Res. 1985; 40: 201–208
   Google Scholar
• Murata T., Hatayama I., Satoh K., Tsuchida S., Sato K. Activation of rat glutathione transferase in class Mu by active oxygen species. Biochem. Biophys. Res. Commun. 1990; 171: 845–851
   PubMed Web of Science ®Google Scholar
• Nishihara T., Maeda H., Okamoto K., Oshida T., Mizoguchi T., Terada T. Inactivation of human placenta glutathione S‐transferase by SH/SS exchange reaction with biological disulfides. Biochem. Biophys. Res. Commun. 1991; 174: 580–585
   PubMed Web of Science ®Google Scholar
• Nishinaka T., Terada T., Nanjo H., Okamoto K., Nishikawa J., Mizoguchi T., Nishihara T. Characterization of lens glutathione S‐transferases. J. Pharmacobio‐Dyn. 1992; 15: s–16
   Google Scholar
• Nishinaka T., Terada T., Nanjo H., Mizoguchi T., Nishihara T. Difference in glutathione S‐transferase response to various oxidative stress between porcine and bovine lens. Exp. Eye Res. 1993, (in press)
   PubMed Web of Science ®Google Scholar
• Habig W. H., Pabst M. J., Jakoby W. B. Glutathione S‐transferases: the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 1974; 249: 7130–7139
   PubMed Web of Science ®Google Scholar
• Habig W. H., Jakoby W. B. Assays for differentiation of glutathione S‐transferases. Methods Enzymol. 1981; 77: 398–405
   PubMedGoogle Scholar
• Lawrence R. A., Burk R. F. Glutathione peroxidase activity in selenium‐deficient rat liver. Biochem. Biophys. Res. Commun. 1976; 71: 952–958
   PubMed Web of Science ®Google Scholar
• Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein‐dye binding. Anal. Biochem. 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 4350–4354
   PubMed Web of Science ®Google Scholar
• Ding G. J.‐F., Lu S. Y.H., Pickett C. B. Rat liver glutathione S‐transferases. Nucleotide sequence analysis of a Yb1 cDNA clone and prediction of the complete amino acid sequence of the Yb1 subunit. J. Biol. Chem. 1985; 260: 13268–13271
   PubMed Web of Science ®Google Scholar
• Ding G. J.‐F., Ding V. D.‐H., Rodkey J. A., Bennet C. D., Lu S. Y.H., Pickett C. B. Rat liver glutathione S‐transferase. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNA by phenobarbital. J. Biol. Chem. 1986; 261: 7952–7957
   PubMed Web of Science ®Google Scholar
• Sugioka Y., Kano T., Okuda A., Sakai M., Kitagawa T., Muramatsu M. Cloning and the nucleotide sequence of rat glutathione S‐transferase P cDNA. Nucleic Acids Res. 1985; 13: 6049–6057
   PubMed Web of Science ®Google Scholar
• Kano T., Sakai M., Muramatsu M. Structure and expression of a human class pi glutathione S‐transferase messenger RNA. Cancer Res. 1987; 47: 5626–5630
   PubMed Web of Science ®Google Scholar
• van Heyningen R., Pirie A. The metabolism of naphthalene and its toxic effect on the eye. Biochem. J. 1967; 102: 842–852
   PubMed Web of Science ®Google Scholar
• Saneto R. P., Awasthi Y. C., Srivastava S. K. Interrelationship between cationic and anionic forms of glutathione S‐transferases of bovine ocular lens. Biochem. J. 1980; 191: 11–20
   PubMed Web of Science ®Google Scholar
• Harding J. J. Free and protein‐bound glutathione in normal and cataractous human lenses. Biochem. J. 1970; 117: 957–960
   PubMed Web of Science ®Google Scholar
• Lou M. F., Dickerson J. E., Jr, Garadi R. The role of protein‐thiol mixed disulfides in cataractogenesis. Exp. Eye Res. 1990; 50: 819–826
   PubMed Web of Science ®Google Scholar
• Zigman S. Photochemical mechanisms in cataract formation. Mechanisms of Cataract Formation in the Human Lens, G. Duncan. Academic Press, London 1981; 117–149
   Google Scholar
• Pirie A. Photo‐oxidation of proteins and comparison of photo‐oxidized proteins with those of the cataractous human lens. Isr. J. Med. Sci. 1972; 8: 1567–1573
   PubMedGoogle Scholar
• Bhuyan K. C., Bhuyan D. K. Regulation of hydrogen peroxide in eye humors; Effect of 3‐amino‐1H‐1,2,4‐triazole on catalase and glutathione peroxidase of rabbit eyes. Biochim. Biophys. Acta 1977; 497: 641–651
   PubMed Web of Science ®Google Scholar