Improved periplasmic production of biologically active murine interleukin-2 in Escherichia coli through a single amino acid change at the cleavage site

摘要: Abstract We fused the mature murine Interleukin-2 (mIL-2) gene to signal peptide of Outer membrane protein A (OmpA). generated mutants mimicking different cleavage sites. hybrid consisting OmpA precisely mIL-2, thereby site native protein, was very poorly secreted into periplasm Escherichia coli (200 U/ml). Insertion a serine residue between and mIL-2 sequence, thus natural site, increased secretion by factor 40,000 (8 × l0 6  U/ml). The specific biological activity equaled that about five times higher than refolded from inclusion bodies. also show temperature at which culture is grown has major impact on level.