Abstract
The mammalian cornea is a rich source of the enzyme, aldehyde dehydrogenase(ALDH; EC1.2.1.3), exhibiting a much higher level of specific activity (per mg of protein or per g of tissue) than liver (Holmes and VandeBerg, 1986; Holmes, 1988). Moreover, bovine (Abedinia et al, 1990), baboon (Algar et al, 1990) and opossum (Holmes et al, 1990) corneal ALDHs represent a major portion of the total soluble protein in each case, and a dual role has been proposed, involving both structural and catalytic properties of this enzyme. It has been well established (see Boettner and Walters, 1962; Zigman, 1983) that the mammalian cornea absorbs damaging UVR, particularly in the wavelength range 290–320nm, and corneal protein has been implicated in this role (Cogan and Kinsey, 1946; see Ringvold, 1980). As a major soluble protein, corneal ALDH may therefore assist in this UV-B absorbing role, as well as perform a catalytic function in the detoxification of UVR-induced peroxidic aldehydes.
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Algar, E.M., Cheung, B., Hayes, J., Holmes, R.S., Beacham, I.R. (1993). Bovine Corneal Aldehyde Dehydrogenases: Evidence for Multiple Gene Products (ALDH3 and ALDHX). In: Weiner, H., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 4. Advances in Experimental Medicine and Biology, vol 328. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2904-0_17
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DOI: https://doi.org/10.1007/978-1-4615-2904-0_17
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