Characterization of sheep liver N-acetyltransferase


Guray T. , Guvenc T.

BIOCHEMICAL ARCHIVES, cilt.13, ss.107-111, 1997 (SCI İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 13 Konu: 2
  • Basım Tarihi: 1997
  • Dergi Adı: BIOCHEMICAL ARCHIVES
  • Sayfa Sayıları: ss.107-111

Özet

Acetyl-coenzyme A (AcCoA)-dependent arylamine N-acetyltransferase (NAT:EC 2.3.1.5) was isolated from sheep liver and the specific activity was found as 5.3+/-1.4x10(-3) (mean+/-SE, n=8) nmoles/ min/ mg protein. The effects of p-aminobenzoic acid (PABA) and acetylCoA concentrations, pH, amount of enzyme and reaction period, on the enzyme activity were also studied and the optimum conditions for maximum activity of sheep liver NAT was determined. Sulfamethazine (SMZ) was used as a substrate in order to study the polymorphic pattern of the NAT activities in sheep liver. The inhibition studies also showed that N-ethylmaleimide was a potent inhibitor of sheep liver NAT when PABA was used as the substrate.