Identification of arylamine N-acetyltransferase activity in the bovine lens.
Arylamine N-acetyltransferase (NAT) activity was identified and partially characterized in the bovine lens. According to size-exclusion HPLC, the molecular mass of the arylamine NAT is approximately 30-kDa. Based upon substrate specificity analysis, it is best described as an arylamine NAT which has some ability to N-acetylate arylalkylamines. This arylamine NAT acetylates para-aminobenzoic acid thereby demonstrating a monomorphic pattern of N-acetylation. It demonstrates low sensitivity to methotrexate inhibition as indicated by the relatively high IC50 value (470 microM). NAT could be involved in lenticular detoxification of both endogenous amines and exogenous drugs.
Laboratory of Retinal Cell and Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
S J
SJ
Gaudet
P
P
Razavi
G J
GJ
Caiafa
G J
GJ
Chader
D010129:4-Aminobenzoic Acid / Q000378:metabolism; D000107:Acetylation; D000818:Animals; D001191:Arylamine N-Acetyltransferase / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007908:Lens, Crystalline / Q000187:drug effects / Q000201:enzymology*; D008727:Methotrexate / Q000494:pharmacology; D008970:Molecular Weight; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D001191:Arylamine N-Acetyltransferase; D010129:4-Aminobenzoic Acid; D008727:Methotrexate