PRODUCTION AND PURIFICATION OF JAPANESE-QUAIL OVALBUMIN AS FUSION PROTEIN WITH GLUTATHIONE-S-TRANSFERASE IN ESCHERICHIA-COLI

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