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Arylamine N-acetyltransferase in human red blood cells
- Source :
- Biochemical Pharmacology. 44:1099-1104
- Publication Year :
- 1992
- Publisher :
- Elsevier BV, 1992.
-
Abstract
- N-Acetyltransferase activities associated with erythrocytes from 20 individuals have been determined with p-aminobenzoic acid as substrate. A three-fold variation in Vmax is found. The N-acetyltransferase genotype of the individuals has been determined and there is no correlation between the extent of acetylation measured in the individuals' erythrocytes and the inheritance of alleles at the polymorphic NAT locus. Folate is confirmed to be an inhibitor of arylamine N-acetyltransferase activity measured in erythrocytes. The content of folate in erythrocytes of individuals also varies. The individual with the maximum folate content has the minimum N-acetyltransferase activity. The monomorphic N-acetyltransferase gene from individuals spanning the range of N-acetyltransferase activity have been amplified, using the polymerase chain reaction. The pattern of restriction enzyme digestion of the monomorphic N-acetyltransferase gene with a series of eight restriction enzymes is the same for individuals spanning the activity range of arylamine N-acetyltransferase in their erythrocytes.
- Subjects :
- Erythrocytes
Genotype
Arylamine N-Acetyltransferase
Molecular Sequence Data
Biology
Biochemistry
chemistry.chemical_compound
Folic Acid
medicine
4-Aminobenzoic acid
Humans
Allele
Gene
Pharmacology
chemistry.chemical_classification
Base Sequence
Arylamine N-acetyltransferase
Gene Amplification
DNA Restriction Enzymes
Molecular biology
Kinetics
Red blood cell
Restriction enzyme
Methotrexate
Enzyme
medicine.anatomical_structure
chemistry
4-Aminobenzoic Acid
Subjects
Details
- ISSN :
- 00062952
- Volume :
- 44
- Database :
- OpenAIRE
- Journal :
- Biochemical Pharmacology
- Accession number :
- edsair.doi.dedup.....9e328ca51a2166de081d327d6ec4cf1a
- Full Text :
- https://doi.org/10.1016/0006-2952(92)90373-q