标题:日本血吸虫SjPP基因原核表达蛋白的酶活性

作者:姚利晓,王欣之,傅志强,陶丽红,林矫矫

作者单位:中国农业科学院上海兽医研究所,农业部动物寄生虫学重点开放实验室,上海动物生物技术研究中心,西南大学柑桔研究所,中国农业科学院柑桔研究所

摘要:分别以磷酸苏氨酸多肽(K-R-pT-I-R-R)和4-硝基苯基磷基二钠盐(pNPP)为底物,研究原核表达的日本血吸虫丝/苏氨酸蛋白磷酸酶重组蛋白rSjPP的酶活性,检测二价金属阳离子(Mn2+、Ni2+、Mg2+、a2+)、温度、pH值对rSjPP酶活性的影响。结果显示,rSjPP重组蛋白可以有效地水解磷酸苏氨酸多肽,具有丝/苏氨酸蛋白磷酸酶活性。rSjPP酶活性的最适温度为60℃,最适pH值为8.0。1~4mmol/LNi2+对rSjPP酶活力有促进作用,但Mn2+、Mg2+、Ca2+等阳离子对rSjPP的酶活力影响不大。

关键词:日本血吸虫,丝/苏氨酸蛋白磷酸酶,酶活性,影响因子

Title: Enzymatic activities of the protein expressed-prokaryoticly in Escherichia coli from SjPP gene of Schistosoma japonicum

Authors: YAO Li-xiao,WANG Xin-zhi,FU Zhi-qiang,TAO Li-hong,LIN Jiao-jiao

Abstract: Using phosphothreonine polypeptide K-R-pT-I-R-R as substrate,the activities of Ser/Thr protein phosphatase(rSjPP) of Schistosoma japonicum expressed in Escherichia coli were tested.The effects of temperature,pH value,divalent cations(Mn2+,Ni2+,Mg2+,and Ca2+) on the enzymatic activities of the rSjPP were analyzed using pNPP as substrate.The phosphothreonine polypeptide could been hydrolyzed by the rSjPP,indicating that the rSjPP possessed the characteristics of Ser/Thr protein phosphatase.Using pNPP as substrate,rSjPP had the strongest catalytic activities under the condition of pH8.0 and 60 ℃.The activities of rSjPP could be enhanced by adding Ni2+ from 1 mmol/L to 4 mmol/L but not by Mn2+,Mg2+,and Ca2+.

Key words: Schistosoma japonicum; Ser/Thr protein phosphatase; enzymatic activity; impact factor;

文献注录:姚利晓,王欣之,傅志强,陶丽红,林矫矫. 日本血吸虫SjPP基因原核表达蛋白的酶活性 [J]. 中国兽医科学. 2008, 07: 555-558.

基金: 国家高技术研究发展计划(863)项目(2006AA10A207);国家“十一五”科技支撑计划项目(2006BAD06A09)

报/刊名:中国兽医科学》,发表于2008 / 第 07 期。

文献类型: [J]

页码: 555-558 页 / 共4

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