Characterization of sheep liver N-acetyltransferase

Date

1997-05-01

Author

Güray, Nülüfer Tülün

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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.

Subject Keywords

ARYLAMINE, MICE

URI

https://hdl.handle.net/11511/56033

Journal

BIOCHEMICAL ARCHIVES

Collections

Department of Biology, Article

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Citation Formats

N. T. Güray, “Characterization of sheep liver N-acetyltransferase,” BIOCHEMICAL ARCHIVES, pp. 107–111, 1997, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/56033.