Abstract
UV irradiation can damage ocular lens proteins and inactivate lens enzymes (Li et al., 1990; Zigman et al., 1991; Rafferty et al., 1993; Hightower, 1995). We have previously reported that bovine lens aldose reductase activity is enhanced by UV irradiation under relatively high D-fructose conditions (Mizoguchi et al., 1996). In our study on the photoreactivity of lens proteins, we have observed that significant amounts of lens protein mixed disulfides with GSH are formed when crude pig lens extract is UV irradiated for 3 min. To determine whether the protein mixed disulfides formed with GSH are sensitive or resistant to proteolysis and to gain insight into the physiological role of lens protein mixed disulfides, we have monitored calpain proteolysis of aldose reductase mixed disulfides with GSH.
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Mizoguchi, T., Maeda, I., Yagi, K., Kador, P.F. (1999). Formation of Lens Aldose Reductase Mixed Disulfides with GSH by UV Irradiation and Its Proteolysis by Lens Calpain. In: Weiner, H., Maser, E., Crabb, D.W., Lindahl, R. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 7. Advances in Experimental Medicine and Biology, vol 463. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4735-8_60
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DOI: https://doi.org/10.1007/978-1-4615-4735-8_60
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