[1]蒋正宁,赵仁慧,吴旭江,等.簇毛麦谷胱甘肽硫转移酶基因HvGSTF 的原核表达与酶活性鉴定[J].江苏农业学报,2016,(06):1219-1222.[doi:doi:10.3969/j.issn.1000-4440.2016.06.004]
 JIANG Zheng-ning,ZHAO Ren-hui,WU Xu-jiang,et al.Prokaryotic expression of a glutathione S-transferase gene HvGSTF from Haynaldia villosa and the enzyme activity[J].,2016,(06):1219-1222.[doi:doi:10.3969/j.issn.1000-4440.2016.06.004]
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簇毛麦谷胱甘肽硫转移酶基因HvGSTF 的原核表达与酶活性鉴定()
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江苏农业学报[ISSN:1006-6977/CN:61-1281/TN]

卷:
期数:
2016年06期
页码:
1219-1222
栏目:
遗传育种·生理生化
出版日期:
2017-02-07

文章信息/Info

Title:
Prokaryotic expression of a glutathione S-transferase gene HvGSTF from Haynaldia villosa and the enzyme activity
作者:
蒋正宁1赵仁慧1吴旭江1别同德1高德荣1张伯桥12
(1.江苏里下河地区农业科学研究所/农业部长江中下游小麦生物与遗传改良重点实验室,江苏扬州225007;2.江苏里下河地区农业科学研究所/现代作物生产协同创新中心,江苏扬州225007)
Author(s):
JIANG Zheng-ning1ZHAO Ren-hui1WU Xu-jiangBIE Tong-de1GAO De-rong1ZHANG Bo-qiao12
(1. Key Laboratory of Wheat Biology and Genetic Improvement in Low & Middle Yangtze River Valley Winter Wheat Region,Ministry of Agriculture/Institute of Agricultural Science of the Lixiahe District in Jiangsu Province, Yangzhou 225007, China;2. Institute of Agricultural Science of the Lixiahe District in Jiangsu Province/Jiangsu Collaborative Innovation Center for Modern Crop Production, Yangzhou 225007, China)
关键词:
簇毛麦谷胱甘肽硫转移酶HvGSTF基因谷胱甘肽过氧化物酶活性氧
Keywords:
Haynaldia villosaglutathione S-transferase (GST)HvGSTF geneglutathione peroxidase (GPX)reactive oxygen species
分类号:
Q786
DOI:
doi:10.3969/j.issn.1000-4440.2016.06.004
文献标志码:
A
摘要:
簇毛麦谷胱甘肽硫转移酶基因(HvGSTF)是1个受白粉病诱导增强表达基因,本研究将其构入原核表达载体pET-28a,在大肠杆菌中表达后,分离纯化重组蛋白HvGSTF,并对其进行活性鉴定。重组蛋白HvGSTF的分子量为29 200,浓度为0.84 mg/ml。重组蛋白HvGSTF具有谷胱甘肽硫转移酶(GST)活性和谷胱甘肽过氧化物酶(GPX)双重活性,酶活力分别为 (5.32±0.22) U/mg和 (20.54±0.42) mU/mg。HvGSTF可能参与了簇毛麦与白粉病互作,但是否参与了簇毛麦受白粉菌侵染后产生的活性氧的清除与调节仍需进一步验证。
Abstract:
HvGSTF, a class glutathione S-transferase gene from Haynaldia villosa, is induced for expression by Blumeria graminis f.sp. tritici infection. In this study, HvGSTF gene was constructed into the vector pET-28a. After expression in Escherichia coli, recombinant protein HvGSTF was purified and detected for enzyme activity. The molecular weight of recombinant HvGSTF was 29 200, and the protein concentration was 0.84 mg/ml. Enzyme assays revealed that HvGSTF was a glutathione S-transferase (GST) with the activity of glutathione reductase (GPX). The activities of GST and GPX were (5.32±0.22) U/mg and (20.54±0.42) mU/mg, respectively. The results imply that HvGSTF might have participated in the interaction between Haynaldia villosa and B.graminis f. sp. tritici because of its dual activities of both GST and GPX. It is unclear whether HvGSTF might have played a role in scavenging reactive oxygen species after infection.

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备注/Memo

备注/Memo:
收稿日期:2016-01-28 基金项目:江苏省自然科学青年基金项目(BK20140500);江苏省农业科技自主创新资金项目[CX(13)2022] 作者简介:蒋正宁(1979-),男,江西乐平人,博士,助理研究员,主要从事小麦分子遗传学研究。(Tel)13665219751;(E-mail)znjiang79@aliyun.com; 通讯作者:张伯桥,(E-mail)zbq@wheat.org.cn
更新日期/Last Update: 2017-02-07