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Identification of a membrane-bound hydrogenase of Desulfovibrio vulgaris (Hildenborough)
Affiliation:1. Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA;2. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA;3. Department of Microbiology and Immunology, Montana State University, Bozeman, MT 59717, USA;4. Biosciences Center, National Renewable Energy Laboratory, Golden, CO 80401, USA
Abstract:Two hydrogenase activities from Desulfovibrio vulgaris (Hildenborough) could be distinguished immunologically and biochemically. The first activity, described as hydrogenase I, corresponded to the soluble enzyme located in the periplasmic space of D. vulgaris. Hydrogenase I had a high specific activity and was sensitive to inhibition by CO. The second activity, hydrogenase II, was located in the membrane fraction, had a lower specific activity and was not affected by CO. The enzymes exhibited different electrophoretic mobilities in polyacrylamide gels, and reacted differently when exposed to proteases. Antibodies raised against purified periplasmic hydrogenase of D. vulgaris reacted with hydrogenase I, but not with hydrogenase II.
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