文献类型: 外文期刊
作者: Wang, Chunlai 1 ; Liu, Siguo 2 ; Peng, Yonggang 2 ; Shao, Meili 2 ; Wang, Yong 3 ; Gong, Qiang; Chang, Yuehong; Liu 1 ;
作者机构: 1.Chinese Acad Agr Sci, Vet Res Inst, Natl Key Lab Vet Biotechnol, Div Bacterial Dis, Harbin 150001, Peoples R China
2.Chinese Acad Agr Sci, Vet Res Inst, Natl Key Lab Vet Biotechnol, Div Bacterial Dis, Harbin 150001, Peoples R China; Heilongjiang Acad Agr Sci, Anim Husbandry Res Ctr, Harbin 150086, Peoples R China; NE Forestry Univ, Harbin 150040, Peoples R China
3.Chinese Acad Agr Sci, Vet Res Inst, Natl Key Lab Vet Biotechnol, Div Bacterial Dis, Harbin 150001, Peoples R China; Heilongjiang Acad Agr Sci, Anim Husbandry Res
关键词: expression;renaturation;purification;ApxII toxin;hemolytic activity;PORCINE CONTAGIOUS PLEUROPNEUMONIA;ESCHERICHIA-COLI;RTX-TOXINS;VIRULENCE;SEROTYPE-1;EXPRESSION;PIGS;HEMOLYSINS;SUBUNIT;OPERONS
期刊名称:PROTEIN EXPRESSION AND PURIFICATION ( 影响因子:1.65; 五年影响因子:1.548 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: ApxII toxin is the only Apx toxin that is produced by Actinobacillus pleuropneumoniae serotype 7. In order to determine whether the recombinant ApxII that derived from Escherichia coli (E. coli) expression is faithful to the natural ApxII so that can be used as additional component in vaccine preparation, the structure gene apxIIA of ApxII toxin was expressed in E coli with prokaryotic expression vector pGEX-6p-1 (formed pGEX-6p-A). pGZRS-C which is A. pleuropneunionicte-E. coli shuttle vector pGZRS-38 expressing the post-transcriptional activation gene apxII C was co-expressed with pGEX-6p-A. The expression product of rApxII A formed inclusion. The inclusion protein was oxidized, refolded and restored hemolytic activity after denaturation, renaturation and purification. The result indicated that E. coli expressed recombinant ApxII toxin has good fidelity, which makes it possible to produce this valuable antigen for vaccine preparation or diagnosis. (c) 2006 Elsevier Inc. All rights reserved.
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