Partial purification and characterization of arylamine N-acetyltransferase in bovine retina
- 1 January 1992
- journal article
- research article
- Published by Taylor & Francis in Current Eye Research
- Vol. 11 (12) , 1185-1192
- https://doi.org/10.3109/02713689208999543
Abstract
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).Keywords
This publication has 10 references indexed in Scilit:
- Rhythmic regulation of retinal melatonin: Metabolic pathways, neurochemical mechanisms, and the ocular circadian clockCellular and Molecular Neurobiology, 1991
- Human ArylamineN-Acetyltransferase Genes: Isolation, Chromosomal Localization, and Functional ExpressionDNA and Cell Biology, 1990
- Evidence for two closely related isozymes of arylamine N‐acetyltransferase in human liverFEBS Letters, 1989
- N-acetyltransferasePharmacology & Therapeutics, 1989
- Purification and physical-chemical properties of acetyl-CoA: Arylamine N-acetyltransferase from pigeon liverBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Retinal rhythms in chicks: circadian variation in melantonin and serotonin N-acetyltransferase activity.Proceedings of the National Academy of Sciences, 1980
- N-acetyltransferase activity responds to environmental lighting in the eye as well as in the pineal glandNature, 1979
- The β-Adrenergic Receptor and the Regulation of Circadian Rhythms in the Pineal GlandPublished by Elsevier ,1977
- Sensitive assay for serotonin N-acetyltransferase activity in rat pinealAnalytical Biochemistry, 1972
- IDENTIFICATION OF N‐ACETYL‐α‐ASPARTYLGLUTAMIC ACID IN THE BOVINE BRAINJournal of Neurochemistry, 1966