Abstract
The molybdoenzyme NADH-nitrate reductase (NADH-NR) (EC 1.6.61) has been purified 3400-fold, by a multi-stage procedure,to homogeneity from spinach ( Spinacea oleracea L.). The enzyme had a specific activity of 102 μmol NO − 2 produced min −1 mg −1. Denaturing electrophoresis revealed two subunits of molecular weight 110,000 and 120,000 and was substantially free of proteolytic degradation products. Extinction coefficients of the functional haem were 127 mM at 412 nm (oxidized) and 172 mM at 423 nm (NADH-reduced). A set of monoclonal antibodies was raised to the pure NR. Six selected for further cloning were all γG type and bound to five distinct and one overlapping site on the enzyme. The various activities of the NR (NADH-oxidizing and nitrate-reducing) were differentially inhibited by the monoclonal antibodies. NADH-NR activities of extracts of roots and leaves of a variety of species were inhibited to different extents.
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