Characterization of sheep liver N-acetyltransferase


Guray T. , Guvenc T.

BIOCHEMICAL ARCHIVES, vol.13, no.2, pp.107-111, 1997 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 13 Issue: 2
  • Publication Date: 1997
  • Title of Journal : BIOCHEMICAL ARCHIVES
  • Page Numbers: pp.107-111

Abstract

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.