Characterization of microsomal aniline hydroxylase of rainbow trout, Salmo gairdneri


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

INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, cilt.35, ss.11-15, 1998 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 35 Konu: 1
  • Basım Tarihi: 1998
  • Dergi Adı: INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS
  • Sayfa Sayıları: ss.11-15

Özet

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.