Production and purification of Japanese quail ovalbumin as fusion protein with glutathione S-transferase in Escherichia coli.

Folia Microbiol (Praha)

Laboratory for Genetic Engineering, Slovak Academy of Sciences, Bratislava.

Published: December 1996

A plasmid encoding a fusion protein interlinked by thrombin recognition sequence between glutathione S-transferase and Japanese quail ovalbumin (without 40 amino acid residues from the 5'-end of the ORF) has been constructed, employing the expression system pGEX-2T. The deglycosylated fusion protein (64 kDa) was purified by affinity chromatography on glutathione agarose beads, analyzed by SDS-polyacrylamide gel electrophoresis, immunochemically detected with antiserum raised against Japanese quail ovalbumin and tested for its stability.

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http://dx.doi.org/10.1007/BF02815417DOI Listing

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