Position: Home > Articles > Activity Determination of N-domain of Two Phosphatase from Anabaena sp.PCC 7120
Hubei Agricultural Sciences
2012,51
(7)
1474-1477
鱼腥蓝细菌PCC 7120中两个磷酸酶N端结构域活性分析
作 者：
许兴俭;陈雯莉;王莉
单 位：
华中农业大学生命科学技术学院/农业微生物学国家重点实验室
关键词：
鱼腥蓝细菌(Anabaena sp.);PrpJ1;PrpJ2;N端结构域;磷酸酶活性
摘 要：
为了研究鱼腥蓝细菌(Anabaena sp.)PCC 7120中两个PP2C类蛋白磷酸酶PrpJ1和PrpJ2的磷酸酶活性,将编码两个蛋白N端至跨膜区的基因片段重组到质粒中,转化大肠杆菌进行原核表达,获得了可溶性的PrpJ1up和PrpJ2up蛋白。并且以pNPP为底物测定了所得蛋白的磷酸酶活性,双倒数作图法结果显示PrpJ1up蛋白的Km为0.30 mmol/L,Vmax为7.10 nmol/min;PrpJ2up蛋白的Km为0.24 mmol/L,Vmax为0.43 nmol/min。
译 名：
Activity Determination of N-domain of Two Phosphatase from Anabaena sp.PCC 7120
作 者：
XU Xing-jian,CHEN Wen-li,WANG Li(College of Life Science and Technology/State Key Laboratory of Agricultural Microbiology,Huazhong Agricultural University, Wuhan 430070,China)
关键词：
Anabaena sp.PCC 7120;PrpJ1;PrpJ2;N-domain;phosphatase activity
摘 要：
The gene fragments encoding N-domain of two phosphatase proteins PrpJ1 and PrpJ2 were cloned into pET28a.Soluble proteins PrpJ1up and PrpJ2up were obtained by prokaryotic expression,and then purified by Ni-NTA argrose.The kinetic constants of PrpJ1up and PrpJ2up towards pNPP were determined.The results showed that Km and Vmax of PrpJ1up were 0.30 mmol/L and 7.10 nmol/min respectively;While Km and Vmax of PrpJ2up were 0.24 mmol/L and 0.43 nmol/min respectively.
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