Partial purification and characterization of arylamine N-acetyltransferase in bovine retina.
Arylamine N-acetyltransferase (NAT) activity was partially purified and characterized in bovine retina. Upon examining the retinal supernatant for multiple ionic species, only one NAT activity was detected. Based upon its substrate specificity, it is best described as an arylamine NAT. According to size-exclusion HPLC, the molecular mass of the arylamine NAT is approximately 30-kDa. This arylamine NAT acetylates p-aminobenzoic acid thereby demonstrating a monomorphic pattern of acetylation. The NAT activity demonstrated low sensitivity to methotrexate inhibition as indicated by a high IC50 value (480 microM).
Gaudet
S J
SJ
Laboratory of Retinal Cell and Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892.
Chader
G J
GJ
D000107:Acetylation; D000818:Animals; D001191:Arylamine N-Acetyltransferase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004791:Enzyme Inhibitors; D008727:Methotrexate / Q000494:pharmacology; D008970:Molecular Weight; D012160:Retina / Q000737:chemistry*; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D001191:Arylamine N-Acetyltransferase; D008727:Methotrexate