• Korean Journal of Microbiology
• /
• v.29 no.5
• /
• pp.296-300
• /
• 1991

The membrane-bound Escherichia coli hydrogenases were purified partially by the solubilization with detergents. the E. coli crude extract was solubilized with sodium deoxycholate and dialyzed against the buffer containing Triton X-100. Two different hydrogenases were obtained by the DEAE-cellulose, hydroxyapatite and Sephedex G-200 column chromatography. The one was unstable during purification and contained 70- and 47-kDa polypeptides as major proteins. The other showed high H2-evolving activity and had major polypeptides of Mr 31 and 27. Those polypeptides were detected by the two-dimensional electrophoresis.