Abstract
The glycoprotein E2 sequences of classical swine fever virus (strain p97) were cloned, sequenced and expressed in E. coli. Result from SDS-polyacrylamide gel electrophoresis analysis of expressed proteins revealed the presence of a prominently stained band corresponding to a molecular mass of 61 kDa, which is in agreement with the predicted size from the DNA sequence. The recombinant E2 protein contained an aminoterminal tag of six histidines that could be used for purification by the nickel chelate affinity chromatography. The elution fractions of the expressed protein also contain additional bands of 40 and 35 kDa proteins, indicating proteolytic cleavages might occur. Our Western blotting result also supported that the expression of the recombinant E2 protein of the classical swine fever virus were accomplished.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
