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Characterization of antibodies to house fly NADPH-cytochrome P-450 reductase

Insect Biochemistry, ISSN: 0020-1790, Vol: 14, Issue: 2, Page: 163-168
1984
  • 31
    Citations
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  • 6
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Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    31
    • Citation Indexes
      31
  • Captures
    6

Article Description

Antibodies to solubilized and purified NADPH-cytochrome P-450 reductase from house fly microsomes were obtained in rabbits. Evolution of antibody titre was determined by the increasing inhibition of house fly microsomal NADPH-cytochrome c reductase activity by serum samples. An IgG fraction was obtained from the serum by ammonium sulphate precipitation. These antibodies inhibited microsomal NADPH-cytochrome c reductase from insecticide-resistant and susceptible house fly strains as well as from phenobarbital-treated insects. The antibodies were specific for NADPH-cytochrome P-450 reductase because they did not inhibit the NADH-dependent reduction of cytochrome c, dichlorophenolindophenol or ferricyanide. The antibodies distinguished the native NADPH-cytochrome P-450 reductase from the proteolytically processed NADPH-cytochrome c reductase as shown by differential inhibition of solubilized, purified enzymes. The antibodies inhibited microsomal cytochrome P-450 monooxygenase activities such as epoxidation and O-dealkylation, thus confirming the role of NADPH-cytochrome P-450 reductase in these reactions. Cross-reactivity towards the microsomal enzyme of 15 animal species was shown by inhibition of NADPH-cytochrome c reductase activity. Cross-reactivity was high for the enzyme of other Diptera such as a Drosophila melanogaster and Culex pipiens, but was very low for NADPH-cytochrome c reductase from vertebrate sources.

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