ISSN: 0973-7510

E-ISSN: 2581-690X

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.
J Pure Appl Microbiol. 2012;6(4):1609-1613
© The Author(s). 2012
Received: 08/01/2012 | Accepted: 27/02/2012 | Published: 31/12/2012
Abstract

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

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