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Arylamine N-acetyltransferase in human red blood cells

Authors :
Jonathan Gordon
Edith Sim
Dean Hickman
Alison Ward
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.

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