The overall objective of the project is to establish the basic biochemical characteristics of the insect microsomal enzyme system and through comparative studies with mammalian enzymes attempt to uncover differences which might be exploited in the design and development of new insecticides. Specific aims include attempts to solubilize, purify and characterize the major catalytic components (NADPH cytochrome c reductase, cytochrome P-450 and lipid fractions) of control and induced armyworm (Spodoptera eridania) gut microsomes, to further study microsomal enzyme induction and the associated role of DNA-dependent RNA polymerases in the armyworm, and to continue studies on heme (P-450) synthesis and the enzyme delta-aminolevulinic acid synthetase. An important additional aim is to solubilize and characterize the microsomal epoxide hydrase in the armyworm and attempt to assess its relationship to the P-450 mediated oxidases. BIBLIOGRAPHIC REFERENCES: Krieger, R. I., C. F. Wilkinson, L. J. Hicks, and E. F. Taschenberg. 1976. Aldrin epoxidation, dihydroisodrin hydroxylation, and p-chloro-N-methylaniline demethylation in six species of saturniid larvae. J. of Econ. Ent. 69, 1-5.