Characterization of glutathione S-transferases of human cornea.
Two cationic (pIs 9.1 and 7.6) and one anionic (pI 4.4) forms of glutathione S-transferase have been purified to an apparent homogeneity from human cornea using glutathione-linked affinity chromatography and isoelectric focusing. The substrate specificities of the three enzyme forms are significantly different from each other. None of the three forms of human cornea glutathione S-transferase express glutathione peroxidase II activity. Immunological and structural studies reveal that human cornea enzymes have structural similarities with glutathione S-transferases of other human tissues.
D055598:Chemical Phenomena; D002621:Chemistry; D003315:Cornea / Q000201:enzymology*; D005979:Glutathione Peroxidase / Q000378:metabolism; D005982:Glutathione Transferase / Q000302:isolation & purification; D006801:Humans; D007158:Immunologic Techniques
D005979:Glutathione Peroxidase; D005982:Glutathione Transferase