Journal of Pure and Applied MicrobiologyVol. 6 No. 4

Detection and Identification of Dihydrolipoamide Dehydrogenase as a Feroxamine Binding Protein from Streptomyces coelicolor

Shinya Kodani1,2* and Kozo Ochi3

1Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan. 2Graduate School of Science and Technology, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan. 3Department of Life Science, Hiroshima Institute of Technology, Miyake 2-1-1, Saeki-ku, Hiroshima, 731-5193, Japan.

Received on 08 January 2012 and accepted on 27 February 2012



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.

Keywords : Dihydrolipoamide dehydrogenase, Deferoxamine, Streptomyces coelicolor, Affinity column.