title: Characterization of purine hydroxylase I from Aspergillus nidulans.
abstract: Purine hydroxylase I from Aspergillus nidulans was purified 850-fold. The purified preparations exhibited the spectral and catalytic properties, including broad specificity for oxidizing and reducing substrates, typical of molybdenum/flavin/iron-sulphur-containing hydroxylases (oxotransferases).
authors.affiliation: Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Ireland.
authors.forename: R K
authors.initials: RK
authors.lastname: Mehra
authors.forename: M P
authors.initials: MP
authors.lastname: Coughlan
mesh_terms: D001233:Aspergillus nidulans / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007658:Ketone Oxidoreductases / Q000302:isolation & purification*; D009243:NAD / Q000378:metabolism; D013379:Substrate Specificity; D014968:Xanthine Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D009243:NAD; D014968:Xanthine Dehydrogenase; D007658:Ketone Oxidoreductases