Microsomal hydroxylation of aniline in the southern armyworm, Spodoptera eridania

L. B. Brattsten, C. F. Wilkinson, M. M. Root

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Microsomal hydroxylation of aniline in midguts of the southern armyworm, Spodoptera eridania, was found to differ in its requirements for optimal in vitro activity from those of armyworm and rat liver p-chloro N-methylaniline N-demethylase and rat liver aniline hydroxylase. Apparent Km values for armyworm aniline hydroxylase were substantially higher than those for rat liver aniline hydroxylase and the N-demethylase enzymes. The armyworm aniline hydroxylase was inhibited by several mixed-function oxidase inhibitors as well as by aldrin and nicotine and was highly inducible by pentamethylbenzene and phenobarbital.

Original languageEnglish (US)
Pages (from-to)615-620
Number of pages6
JournalInsect Biochemistry
Volume6
Issue number6
DOIs
StatePublished - 1976
Externally publishedYes

Keywords

  • Insect aniline hydroxylation
  • Microsomal induction
  • Microsomal inhibition
  • Mixed-function oxidation

Fingerprint

Dive into the research topics of 'Microsomal hydroxylation of aniline in the southern armyworm, Spodoptera eridania'. Together they form a unique fingerprint.

Cite this