关键词: 马铃薯腐烂茎线虫, 谷胱甘肽过氧化物酶, 基因克隆, 原核表达

Abstract: To further understand the structure and function of glutathione peroxidase, a glutathione peroxidase gene was cloned from plant-parasitic nematode（Ditylenchus destructor）using RACE method, and the gene（DdGpx）was transferred into vector of pET-41b to have the fusion expression. The full-length cDNA of DdGpx was 950 bp containing an open reading frame of 681 bp and encoding 226 amino acids. Bioinformatics analysis indicated that the N terminal of the protein had obvious signal peptide, belonging to the secretory protein. The prokaryotic expression vector pET-41b-DdGpx was constructed and then transformed into BL21（DE3）, there was a apparent band in 60 kD. Mass spectrum analysis indicated that there were 7 peptides matched with D. destructor GPX protein, implying that the recombinant protein of Dd-GPX was successfully expressed

Key words: Ditylenchus destructor, glutathione peroxidase, gene cloning, prokaryotic expression