Partial purification of Cytochrome P450 from Helicoverpa armigera (Hubner)

Abstract

The cytochrome P450 (Cyt-P450) proteins from the fat body and midgut of the cotton bollworm, Helicoverpa armigera, were respectively partially purified by a set of purification procedures including differential centrifugation, solubilization of CHAPS, protein precipitation by PEG precipitation and DE-32 column chromatography. The Cyt-P450 was detected by methods of CO difference spectrum and SDS-PAGE. Fraction of detergent solubilized microsomes from the fat body of H. armigera was purified more than 17-fold. Three protein bands were detected by SDS-PAGE with molecular masses of 70 600, 63 300 and 571 200Da. It is possible that the proteins with molecular mass of 63 300 and 571 200Da were the isozymes of Cyt-P450.