Summary
Certain ocular proteins have been found to be chemically modified by exposure to near-UV light (320–390 nm) in the presence of tryptophan. Colored and fluorescent tryptophan photoproducts bind firmly to proteins, thereby altering their physico-chemical properties. The question of whether such a reaction would inhibit the catalytic action of catalase is herein raised. When solutions of bovine liver catalase were re-incubated up to 24 hr under near-UV with preirradiated tryptophan and dialyzed, most of the ability of the enzyme to decompose H2O2 was lost. Similar results occurred for catalase activities of bovine cornea and lens epithelia. The enzyme protein exhibited altered UV absorption and fluorescence spectra and increased electrophoretic mobility after binding photoproducts. Near-UV light photoproducts of tryptophan are thus capable of deactivating crystalline and tissue catalase.
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Zigman, S., Science 171, 807–809, 1971.
Zigman, S., Schultz, J., Yulo, T., and Grover, D., Israel J. Med. Sci. 8, 1590–1595, 1972.
Zigman, S., Griess, G., Yulo, T., and Schultz, J., Exp. Eye Res. 15, 255–264, 1973.
Zigman, S., Schultz, J., Yulo, T., and Griess, G., Exp. Eye Res. 17, 209–217, 1973.
Deisseroth, A. and Dounce, A., Physiol Rev. 50, 319–375, 1970.
Beers, R. F., and Sizer, I. W., J. Biol. Chem. 195, 133–140, 1952.
Ornstein, L. and Davis, B. J., Disc Electrophoresis Distillation Products Industries, Rochester, New York, 1960.
Liu, T., and Chang, Y., J. Biol. Chem. 246, 2843–2848, 1971.
Nakatani, M., J. Biochem. (Tokyo) 48, 476–482, 1960.
Bhuyan, K. C. and Bhuyan, D. K., American J. Ophthalmology 69, 147–153, 1973.
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Supported by a research grant from The National Eye Institute of the National Institutes of Health (EY-00459).
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Zigman, S., Yulo, T. & Griess, G.A. Inactivation of catalase by near ultraviolet light and tryptophan photoproducts.. Mol Cell Biochem 11, 149–154 (1976). https://doi.org/10.1007/BF01744995
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DOI: https://doi.org/10.1007/BF01744995