Abstract
Oxygenases catalyze the incorporation of either one or two atoms of molecular oxygen into their substrates and are classified into two major groups: mono-oxygenases and di-oxygenases. Indoleamine 2,3-dioxygenase (a superoxygenase) is a unique heme-containing oxygenase, because it requires the superoxide anion for the initiation of the reaction and for the maintenance of the catalytic cycle during the steady state. A dramatic and specific induction of pulmonary indoleamine 2,3-dioxygenase by virus and lipopolysaccharide (LPS) was mediated by interferon, and the interferon-mediated enzyme induction was completely suppressed by the inhibitors of prostaglandin biosynthesis. The antiviral activity of interferon is inhibited by nonsteroidal anti-inflammatory agents, such as indomethacin and aspirin. However, oligoadenylate synthetase or protein kinase induction by interferon, both of which are candidates of antiviral proteins, was not inhibited by these agents. Therefore, indoleamine 2,3- dioxygenase may play an important role in the inflammatory processes, immune responses, and/or the mode of action of interferon. This chapter describes the purification method of rabbit indoleamine 2,3-dioxygenase enzyme.
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