NADH substrate inhibition and enhanced thermal stability of higher plant nitrate reductase immobilized via a monoclonal antibody.
The molecular basis of light-induced circadian rhythms of higher plant NADH:nitrate reductase (EC 1.6.6.1) activity is presently not understood. We have investigated whether the regulatory properties of NADH:nitrate reductase would allow oscillatory or related dynamic behavior. We report here the first example of NADH substrate inhibition of higher plant nitrate reductase in solution and for an immobilized enzyme using a novel immobilization technique with a monoclonal antibody. According to current theories on chemical oscillatory reactions, substrate inhibition will allow bistable and oscillatory behavior when the substrate-enzyme reaction is carried out in an open system. We also found a significant enhanced thermal stability of the immobilized enzyme.
Ruoff
P
P
Department of Biological Sciences, Michigan Technological University, Houghton 49931.
Lillo
C
C
Campbell
W H
WH
D000911:Antibodies, Monoclonal / Q000276:immunology; D000937:Antigen-Antibody Reactions; D004800:Enzymes, Immobilized / Q000378:metabolism; D006358:Hot Temperature; D007700:Kinetics; D009243:NAD / Q000378:metabolism*; D050901:Nitrate Reductase; D009565:Nitrate Reductases / Q000276:immunology / Q000378:metabolism*; D010507:Periodicity; D011489:Protein Denaturation; D003313:Zea mays / Q000201:enzymology
D000911:Antibodies, Monoclonal; D004800:Enzymes, Immobilized; D009243:NAD; D009565:Nitrate Reductases; D050901:Nitrate Reductase