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KMID : 0364819910290050296
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Korean Journal of Microbiology
1991 Volume.29 No. 5 p.296 ~ p.300
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Indentification and Partial Purification of Two Hydrogenase Isoenzymes from Escherichia coli
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Choi, Suk-Jung/최석정
Yang, Chul-Hak/양철학
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Abstract
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1
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.
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