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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).
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© Society for General Microbiology 1989