期刊
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
卷 30, 期 6, 页码 941-946出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/14756366.2014.999236
关键词
Acetylcholinesterase; carbonic anhydrases; enzyme inhibition; hydroquinone; isoenzymes
资金
- EU project of the 7th FP, Metoxia
- EU project of the 7th FP, Dynano
- Deanship of Scientific Research at King Saud University [RGP-VPP-254]
Carbonic anhydrases (CAs) are widespread and the most studied members of a great family of metalloenzymes in higher vertebrates including humans. CAs were investigated for their inhibition of all of the catalytically active mammalian isozymes of the Zn2+-containing CA, (CA, EC 4.2.1.1). On the other hand, acetylcholinesterase (AChE. EC 3.1.1.7), a serine protease, is responsible for ACh hydrolysis and plays a fundamental role in impulse transmission by terminating the action of the neurotransmitter ACh at the cholinergic synapses and neuromuscular junction. In the present study, the inhibition effect of the hydroquinone (benzene-1,4-diol) on AChE activity was evaluated and effectively inhibited AChE with K-i of 1.22 nM. Also, hydroquinone strongly inhibited some human cytosolic CA isoenzymes (hCA I and II) and tumour-associated transmembrane isoforms (hCA IX, and XII), with K(i)s in the range between micromolar (415.81 mu M) and nanomolar (706.79 nM). The best inhibition was observed in cytosolic CA II.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据