| First Author | Downes JE | Year | 1993 |
| Journal | Biochem Mol Biol Int | Volume | 30 |
| Issue | 3 | Pages | 525-35 |
| PubMed ID | 8401311 | Mgi Jnum | J:14483 |
| Mgi Id | MGI:62650 | Citation | Downes JE, et al. (1993) Purification and properties of murine corneal aldehyde dehydrogenase. Biochem Mol Biol Int 30(3):525-535 |
| abstractText | Murine corneal aldehyde dehydrogenase has been purified to homogeneity and characterized with a range of aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit molecular weight of 59 KDa. and appears to prefer aldehyde products of lipid peroxidation as substrates. The enzyme constituted approximately 5% of the total soluble protein of mouse cornea. A dual role has been proposed for corneal aldehyde dehydrogenase in providing the eye with protection against UV-B light: by oxidizing aldehydes generated through light-induced lipid peroxidation; and by the direct absorption of UV-B light by the enzyme. |
