Abstract
Optimal conditions were established for the isolation and storage of microsomal NADPH-cytochrome c reductase from midgut tissues of southern armyworm ( Spodoptera eridania) larvae. Compared with KCl (1.15%)-nicotinamide (0.2%), the use of an isolation medium consisting of sucrose (0.25 M), phenylmethane sulphonyl fluoride (0.5 mM), polyvinylpyrrolidone (1%) and EDTA (1 mM) increased by 1.7-fold the yield of reductase activity in the microsomal fraction. Washing microsomes isolated in the sucrose medium with sucrose (0.3 M)-pyrophosphate (0.1 M) removed 30% of the protein and caused a similar increase in the specific activity of the reductase. Characteristics of the midgut microsomal NADPH-cytochrome c reductase were similar to those of the rat liver microsomal enzyme except that the former was relatively insensitive to changes in ionic strength.
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