Characterization of enolase fromClostridium difficile |
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Authors: | Dr Gaynor A Green Raymonde Girardot Olivier Baldacini Marc Ledig Henri Monteil |
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Institution: | (1) Center of Neurochemistry, CNRS, Strasbourg, France;(2) Institut de Bactériologie de la Faculté de Médecine, 3, rue Koeberlé, 67000 Strasbourg, France |
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Abstract: | We have isolated and purified enolase fromClostridium difficile. This is the first report of an enolase of theClostridium genus, and in general its characteristics resemble those described previously for other species, except that it is extremely thermostable. Interestingly,C. difficile enolase has an octameric structure (approximately 300 kDa on native PAGE, 50 kDa on SDS PAGE, and 338 kDa by gel filtration). Enolases fromC. sordellii andC. bifermentans have been partially purified and have a molecular weight similar to that ofC. difficile. It may be that this large size is common for enolases isolated from bacteria of theClostridium genus. |
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