Optimization of conditions for expression of recombinant interferon-y in XXXX .

@entity1 @entity1522 @entity19 @entity2348 @entity379 @entity526
@entity379 ) is an important immunoregulatory cytokine that has a central role against viral and @entity2348 . In this study, the cDNA encoding 141 @entity1522 of mature @entity379 from @entity19 splenocytes was cloned in a prokaryotic expression vector pQE 30. Optimization of expression conditions resulted in high @entity379 protein. Western blot showed that recombinant @entity379 was specifically recognized by its counterpart anti-mouse @entity379 antibodies. In vitro dose-dependent studies, with A549 and HeLa cell lines, showed that cloned @entity379 was safe and had no effect on cell proliferation. The protein prediction and analysis using SOPMA program, revealed that @entity379 had 80 a-helices, 8 b-turns jointed by 9 extended strands and 44 random coils. A total of four major clusters were observed with @entity19 @entity379 sharing 39 % homology with @entity1 @entity379 . Pair-wise alignment studies with @entity1 revealed 26 % identity and 43.3 % similarity. The recovery of bioactive proteins from inclusion bodies (IBs) is a complex process and various protocols have been developed. We report here a simple, robust and inexpensive purification approach for obtaining recombinant @entity379 protein expressed as IBs in @entity526 .
