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Natural variation in the expression of cytochrome P-450 and dimethylnitrosamine demethylase in Drosophila

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
Electrophoresis of Drosophila microsomes resolves two major hemecontaining protein bands with apparent molecular weights of 59,290 (band a) and 55,750 (band b). The hemoproteins in these two bands can account for most of the cytochrome P-450 in the organism. Band a is present in all strains examined: band b is not. Dimethylnitrosamine demethylase, a P-450 enzyme, is a component of band b. Numerous studies have shown that P-450-attributed activities of Drosophila are genotype dependent. Drosophila, therefore, represents a unique system for studying the genetics of, and the molecular mechanisms that regulate, the expression of constitutive levels of P-450 isozymes. Here we explore the molecular basis for the large differences in P-450 expression between strains. Microsomal proteins from several wild-type strains were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Significant differences in the protein bands that contained P-450 were observed between strains with high or low mixed-function oxidase activity. 22 references, 2 figures, 1 table.
Research Organization:
Oak Ridge National Lab., TN
DOE Contract Number:
AC05-84OR21400
OSTI ID:
5871800
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 123:3; ISSN BBRCA
Country of Publication:
United States
Language:
English

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