Purification and characterization of NADPH-cytochrome P450 reductase from Lake Van fish liver microsomes and investigation of some chemical and metals' effects on the enzyme activity
Abstract
NADPH-cytochrome P450 reductase was purified from Lake Van fish liver
microsomes by primary and secondary DEAE-cellulose column chromatograph
with 20.46 mu M/min/mg enzyme specific activities, 54.4\% purification
yield, and purification of 38-fold. The purity of the enzyme was
established, and its monomer molecular weight was determined by
SDS-polyacrylamide gel electrophoresis. SDS-PAGE results showed a single
band and the molecular weight of NADPH-cytochrome P450 reductase was 70
kDa. In addition, optimum ionic strength, optimum pH, optimum
temperature, and stable pH values were determined for the enzyme in the
kinetic studies performed. K-M and V-max were determined for NADPH and
cytochrome c. Effects of some metals ions, antibiotics, and some other
drugs used in aquarium fisheries on the activity of the enzyme were
investigated. IC50 values and K-i values of metals showing an inhibitory
effect were calculated.
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