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Structural and Functional Changes in Catalase Induced by Near‐UV Radiation
Author(s) -
Zigman Seymour,
Reddan John,
Schultz Joanne B.,
McDaniel Thurma
Publication year - 1996
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1996.tb09637.x
Subject(s) - catalase , chemistry , biochemistry , enzyme , biophysics , biology
Part one of this study shows that exposure of purified beef liver catalase in buffered solutions to BL lamps that provide a mixture of 99% UVA and 1% UVB (to be labeled UV A ) alters its chemistry and enzymatic activity. Thus, its spectral absorbance lost detail, it aggregated and exhibited a lower isoelectric point and its enzymatic activity was substantially reduced. These photochemically induced changes were increased by irradiation in phosphate buffer or in physiological medium (minimal essential medium) containing riboflavin and tryptophan. Neither α‐tocopherol nor de‐feroxamine were protective against these UV A ‐induced changes in pure catalase. We further investigated the effect of UV A radiation on the activity of catalase in cultured lens epithelial cells and the protective effects of antioxidants. Cultured lens epithelial cells of rabbits and squirrels were exposed to near‐UV radiation with representation in the UVA region of 99% and 1% UVB. Catalase assays were done on ho‐mogenate supernatants of cells kept dark or UV exposed. In some instances, cells were cultured in medium containing a‐tocopherol or deferoxamine prior to UV radiation. Comparisons were made between UV‐exposed lens cell catalase activity when exposure was done with or without the antioxidants. The UV A radiation was strongly inhibitory to both rabbit and squirrel lens epithelial cell catalase activities. The range of fluxes of near UV radiation was compatible with that which could reach the lens from the sunlit environment. Catalase inactivation was lessened in cells preincubated with a‐tocopherol and deferoxamine. This suggests that both singlet oxygen and hydroxyl radical formation may be involved in near‐UV damage to lens epithelial cell catalase. Such inhibition of catalase by near‐UV would enhance H 2 O 2 toxicity and stimulate SH oxidation so as to damage the lens.