Abstract
Xanthine oxidoreductase occurs in mammalian tissues mostly in a NAD+-dependent form1. In rat liver this dehydrogenase form accounts for over 85 % of total enzyme, the rest being an intermediate dehydrogenase-oxidase form which preferably reacts with NAD% but can also use O2as an electron acceptor2. Both these forms are inhibited by NADH2, in contrast to the O2-dependent form3 arising from them2.
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© 1980 Plenum Press, New York
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Jeżewska, M.M., Kamiński, Z.W. (1980). Xanthine Oxidoreductase Inhibition by NADH as a Regulatory Factor of Purine Metabolism. In: Rapado, A., Watts, R.W.E., De Bruyn, C.H.M.M. (eds) Purine Metabolism in Man—III. Advances in Experimental Medicine and Biology, vol 122B. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8559-2_7
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DOI: https://doi.org/10.1007/978-1-4684-8559-2_7
Publisher Name: Springer, Boston, MA
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