As the first step to elucidate the physiological role of siderophore deferoxamine, the binding proteins in the cell of Streptomyces coelicolor were explored by an affinity chromatography. An affinity column was designed using feroxamine as an affinity ligand. As a result of chromatography, one major protein band at 51 kDa, along with traces of minor proteins, was detected in eluted fraction by analysis of SDS-PAGE. The 51k Da protein was identified as putative dihydrolipoamide dehydrogenase using peptide mass fingerprinting method.
Dihydrolipoamide dehydrogenase, Deferoxamine, Streptomyces coelicolor, Affinity column
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