Characterization of microsomal aniline hydroxylase of rainbow trout, Salmo gairdneri


Güner S., Colak A. , Özen T., Şentürk H. B.

INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, vol.35, no.1, pp.11-15, 1998 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 35 Issue: 1
  • Publication Date: 1998
  • Title of Journal : INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS
  • Page Numbers: pp.11-15

Abstract

Aniline hydroxylase from liver microsomes of rainbow trout Salmo gairdneri converted aniline to p-aminophenol, the specific activity being 0.068 nmoles/min/mg protein in potassium phosphate buffer, pH 7.4 at 25 degrees C. The maximal rate of the enzyme reaction was found at aniline concentrations above 5 mM and in the presence of NADPH. V-max and K-m were 0.048 nmoles/min/mg and 0.105 mM respectively. The Hill plot showed the Hill constant to be 1.02 indicating one substrate binding site with no cooperativity. Ca2+ and Mg2+ at concentrations ranging between 1-10 mM stimulated the enzyme activity.