Secretion of Human Superoxide Dismutase in Escherichia Coli

摘要: The gene for human superoxide dismutase (hSOD), a cytoplasmic enzyme, was cloned into high expression, secretion vector, pIN–III–OmpA. Upon induction of the new protein produced at level approximately 10% total cellular protein, which migrated identical position in SDS–polyacrylamide gel electrophoresis as hSOD E. coli cytoplasm. product recovered major component periplasmic fraction. specific enzymatic activity secreted SOD half that expression with non–secretion vector. These results indicate substantial fraction able to be properly folded enzymatically active conformation. This is first report demonstrate foreign can across inner membrane space yielding an enzyme.