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- W2359689374 abstract "Foot-and-mouth disease virus (FMDV) VP1 gene was amplified by RT-PCR. The VP1 fragment was inserted into plasmid pMBX to obtain recombinant plasmid pMBX-VP1. The pMBX-VP1 was transformed into Escherichia coli BL-21(DE3) to induce VP1 gene fusion expression with 1 mmol/L Isopropylthio-β-D-galactoside (IPTG). The fusion protein band with molecular weight of 58 kD was visible on the SDS-PAGE gel. The density scanning showed that the largest amount of the fusion protein was 35.5% of total bacterial protein. The amounts of the soluble form of the fusion in supernatant of lysate was up to 31.2%, and 6.8% in sediment. Western blot result shawed that the expression products could specifically reacted with the antisera against FMDV. The soluble fusion protein was purified by 50%Ni-NTA affinity chromatography and used as an antigen, and FMDV antibody could be detected by ELISA method." @default.
- W2359689374 created "2016-06-24" @default.
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- W2359689374 date "2006-01-01" @default.
- W2359689374 modified "2023-09-27" @default.
- W2359689374 title "High Soluble Expression and Antigenicity of VP1 Gene of Foot-and-mouth disease virus" @default.
- W2359689374 hasPublicationYear "2006" @default.
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