Identification and characterization of arylamine N-acetyltransferase activity from the bovine retinal pigment epithelium
作者:
GaudetStephen J.,
TsilouEkaterini,
ChaderGerald J.,
期刊:
Current Eye Research
(Taylor Available online 1993)
卷期:
Volume 12,
issue 3
页码: 271-278
ISSN:0271-3683
年代: 1993
DOI:10.3109/02713689308999473
出版商: Taylor&Francis
数据来源: Taylor
摘要:
Arylamine N-acetyltransferase (NAT) activity was identified and characterized in bovine retinal pigment epithelium (RPE) cells. Upon examining the RPE supernatant for multiple ionic species, one major NAT activity peak was detected. Based upon its substrate specificity, it is best described as an arylamine NAT. However, there was detectable arylalkylamine NAT activity within this peak. Further purification via size-exclusion HPLC revealed multiple peaks of NAT activity, although the major peak (around 30 kDa) again predominantly exhibits arylamine NAT activity. However, substrate specificity studies indicate that this arylamine NAT activity is able to acetylate specific arylalkylamine substrates. This arylamine NAT demonstrates a monomorphic pattern of acetylation since it acetylates p-aminobenzoic acid rather than sulfamethazine. It also demonstrates a low sensitivity to methotrexate inhibition indicated by the high IC50value (570μM). The mode of inhibition by methotrexate is uncompetitive as demonstrated by kinetic analysis.
点击下载:
PDF (575KB)
返 回