Production of Soluble and Active Recombinant Murine Interleukin-2 in Escherichia coli: High Level Expression, Kil-Induced Release, and Purification

摘要: We describe the production of soluble murine interleukin-2 (mIL2) and its purification following regulated release in growth medium Escherichia coli. The system is based on ability Kil protein pMB9 to periplasmic proteins into medium. As kil gene under control strong, but well regulatable pL promoter, bearing plasmid stably maintained cell. mIL2, fused outer membrane A (OmpA) signal peptide, was secreted periplasm subsequently released after induction gene. This strategy allows a quick easy heterologous without using strong denaturants or detergents, yielding native with specific biological activity equal natural mIL2. permits mIL2 at levels up 16 mg/liter. From 12-liter fermentation, final yield about 30 mg pure obtained.