title: Xanthine:NAD+ oxidoreductase from embryo liver of hen Gallus gallus.
abstract: 1. Xanthine:NAD+ oxidoreductase from chick embryo liver is unconvertible to the O2-dependent form, as is the enzyme from the adult hen. The Km for NAD+ (approximately 3 microM) of the embryonic enzyme is equal to, and the Km for xanthine (approximately 5 microM) is 2.5-fold lower, when compared with respective Km values of the "adult" hen enzyme. The inhibition of embryonic enzyme by NADH begins at 10 microM NADH and attains 13% at 35 microM NADH (respective data for the "adult" enzyme: 50 microM and 20% at 80 microM NADH). 2. The course of hypoxanthine----xanthine----uric acid hydroxylation catalyzed by the embryonic and "adult" enzymes is similar, however the rate of the first reaction is 2-fold lower for the embryonic enzyme. Under conditions of the limited nutritional system in the developing chick embryo, the low rate of hypoxanthine hydroxylation may promote reutilization of hypoxanthine for nucleotide synthesis.
authors: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
authors: B
authors: B
authors: Zakrzewska
authors: M M
authors: MM
authors: Jezewska
mesh_terms: D000818:Animals; D002642:Chick Embryo; D005260:Female; D006900:Hydroxylation; D007700:Kinetics; D008099:Liver / Q000196:embryology / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D014968:Xanthine Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*
chemical_list: D009243:NAD; D014968:Xanthine Dehydrogenase