title: Purification of aldehyde oxidase from bovine ciliary body.
abstract: Ocular aldehyde oxidase was purified for the first time from bovine ciliary body cytosol by ammonium sulfate fractionation and successive HPLC using DEAE anion-exchange and hydroxyapatite columns. The purified enzyme was homogeneous by the criterion of sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be about 150,000 by electrophoresis and to be about 300,000 by gel filtration HPLC on a TSK gel G3000SWXL column, indicating that the enzyme consists of two subunits with the same molecular weight. On the other hand, nicotinamide N-oxide reductase activity was associated with aldehyde oxidase activity throughout the purification steps of the latter enzyme. This fact indicated that nicotinamide N-oxide reductase activity of the ciliary body cytosol is due to aldehyde oxidase present in the tissue preparation.
authors: Department of Ophthalmology, Hiroshima University School of Medicine, Japan.
authors: S
authors: S
authors: Shimada
authors: H K
authors: HK
authors: Mishima
authors: H
authors: H
authors: Nikaido
authors: S
authors: S
authors: Kitamura
authors: K
authors: K
authors: Tatsumi
mesh_terms: D042931:Aldehyde Oxidase; D000445:Aldehyde Oxidoreductases / Q000032:analysis / Q000302:isolation & purification*; D000818:Animals; D002417:Cattle; D011232:Chemical Precipitation; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D002924:Ciliary Body / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight
chemical_list: D000445:Aldehyde Oxidoreductases; D042931:Aldehyde Oxidase