Xanthine dehydrogenase from Drosophila melanogaster: purification and properties of the wild-type enzyme and of a variant lacking iron-sulfur centers.

Abstract excerpt

Xanthine dehydrogenase has been purified to homogeneity by conventional procedures from the wild-type strain of the fruit fly Drosophila melanogaster, as well as from a rosy mutant strain (E89----K, ry5231) known to carry a point mutation in the iron-sulfur domain of the enzyme. The wild-type enzyme had all the specific properties that are peculiar to the molybdenum-containing hydroxylases. It had normal contents...

Topics

• Animals
• Drosophila melanogaster
• Electron Spin Resonance Spectroscopy
• Enzyme Activation
• Flavin-Adenine Dinucleotide
• Iron-Sulfur Proteins
• Isoenzymes
• Kinetics
• Molecular Weight
• Molybdenum
• Mutation