Abstract
The natural human H-chain ferritin was expressed in E. coli using a multi-copy expression vector containing the λ p L promoter. A variant H-ferritin, having an altered N-terminus, was also produced. These proteins are overproduced (> 30% of the soluble protein), correctly assembled into its 24-subunit shell, and able to bind iron. The identity of the products was confirmed using an antibody specific for H-ferritin.
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