title: Purification and partial characterization of chicken liver acetyl coenzyme A: arylamine N-acetyltransferase.
abstract: Arylamine acetyltransferase (EC 2.3.1.5) was purified 120-fold from chicken liver. The enzyme showed a rise in activity from pH 6.5 to 7.7 followed by a constant activity to about pH 8.6. The relative molecular weight of the enzyme was about 34,000. The apparent Km for acetyl-CoA was 13 microM with 4-nitroaniline as acetyl-acceptor. CoA was a noncompetitive inhibitor relative to acetyl-CoA with apparent Ki value of 110 microM. With 4-methylaniline as substrate, arylamine acetyltransferase activity in pigeon liver was about 8 times greater than in chicken liver, and about 40 times greater than in rabbit.
mesh_terms: D000123:Acetyltransferases / Q000302:isolation & purification*; D000818:Animals; D001191:Arylamine N-Acetyltransferase / Q000302:isolation & purification* / Q000378:metabolism; D002645:Chickens; D010856:Columbidae; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011817:Rabbits; D051381:Rats; D013045:Species Specificity
chemical_list: D000123:Acetyltransferases; D001191:Arylamine N-Acetyltransferase