Purification and properties of murine corneal aldehyde dehydrogenase.
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.
Downes
J E
JE
Division of Science and Technology, Griffith University, Nathan, Brisbane, Australia.
Holmes
R S
RS
D000444:Aldehyde Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D000447:Aldehydes / Q000378:metabolism; D000818:Animals; D002846:Chromatography, Affinity; D003315:Cornea / Q000201:enzymology* / Q000528:radiation effects; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism; D051379:Mice; D008970:Molecular Weight; D013379:Substrate Specificity; D014466:Ultraviolet Rays
D000447:Aldehydes; D007527:Isoenzymes; D008054:Lipid Peroxides; D000444:Aldehyde Dehydrogenase