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Bulletin of Botanical Research ›› 2011, Vol. 31 ›› Issue (6): 692-695.doi: 10.7525/j.issn.1673-5102.2011.06.009

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Characteristics of Recombined Protein GST-OsCATB Expressed in E.coli

LIU Da-Li;;LU Zhen-Qiang;*;ZHANG Ge-Yan;YU Ting-Ting;WANG Xu   

  1. 1.Key Laboratory of Molecular Biology,of Heilongjiang Provincial,College of Life Sciences,Heilongjiang University,Harbin 150080;2.Key Laboratory of Sugar Beet Genetics and Breeding,Academy of Crop Sciences,Chinese Academy of Agricultural Sciences,Harbin 150080;3.Key Laboratory of Forest Plant Ecology of Northeast Forestry University,Ministry of Education,Harbin 150040
  • Received:1900-01-01 Revised:1900-01-01 Online:2011-11-20 Published:2011-11-20
  • Contact: LU Zhen-Qiang
  • Supported by:

Abstract: To clarify the enzymology of catalase in rice(Oryza sativa L.), large quantities and active of the target protein is available firstly. Here, rice OsCATB(GenBank accession No.D26484) gene was cloned and constructed with the pGEX-6p-3 vector to allow expression of OsCATB as glutathione-S-transferase(GST) fusion protein, and E.coli strain BL21 was used for expression of fusion proteins as well. The results indicated that GST-OsCATB fusion proteins were effectively expressed in E.coli, and regulated by IPTG, inducing period, temperature and others of the actions. The purified, enough and activity GST-OsCATB was obtained by affinity chromatography using glutathione-Sepharose 4B column. The final yield was 51 mg·g-1 dry cells for GST-OsCATB.

Key words: Catalase, rice(Oryza sativa L.), glutathione-S-transferase(GST) fusion protein, purification, Escherichia coli

CLC Number: