Characterization of an ecto-5′-nucleotidase (EC 3.1.3.5) activity in intact trophozoites of Trichomonas gallinae
详细信息查看全文 | 推荐本文 |
摘要
This study describes the enzymatic properties of an ecto-5′-nucleotidase in Trichomonas gallinae. The enzyme hydrolyzes nucleoside monophosphates at pH 7.2 and is activated by divalent cations, such as magnesium. Ecto-5′-nucleotidase activity was insensitive to levamisole, tetramisole (alkaline phosphatase inhibitors), and AMPCP (adenosine 5′-[α,β-methylene]diphosphate), an ecto-5′-nucleotidase inhibitor, whereas 0.1 mM ammonium molybdate (considered a potent inhibitor of 5′-nucleotidase activity) completely inhibited the enzyme activity. The apparent KM (Michaelis constant) and Vmax (maximum velocity) values for Mg2+-AMP were 466 ± 57 μM and 3.7 ± 0.59 nmolPi/min/106 trichomonads, respectively. Considering that trichomonads lack the ability to synthesize purines and pyrimidines de novo, the presence of an ecto-5′-nucleotidase in intact trophozoites of T. gallinae could be important in regulating the extracellular nucleotide levels and generating adenosine, essential for the survival strategies of the parasite.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700