An immunogenic protein with an apparent mol. wt of 80 kDa that was recognised by 55% of sera from patients infected with in Western blots was found in butanol extracts of membranes. The N-terminal amino-acid sequence of the 80-kDa protein showed 80% identity with the N-terminal sequence of subunit A of the fumarate reductase of , suggesting the existence of a fumarate reductase in . The membrane fraction of catalysed succinate oxidation with methylene blue at a specific enzyme activity of 0.06 U/mg of protein. The enzyme was purified by Triton X100 extraction followed by ion-exchange chromatography. The purified enzyme contained an 80-kDa protein which was recognised by rabbit serum raised against subunit A of fumarate reductase of . A second protein band with a mol. wt of 31 kDa was recognised by rabbit serum raised against subunit B of fumarate reductase of . Two-dimensional gel electrophoresis demonstrated that the 80- and 31-kDa proteins were subunits of one protein complex. These results indicate that contains an enzyme that is very similar to fumarate reductase. The 80-kDa subunit was recognised in sonicates of all 32 strains tested by rabbit antibodies raised against subunit A of fumarate reductase of , indicating that fumarate reductase is a common protein in . The fumarate reductase of might enable the bacterium to perform anaerobic respiration in a similar fashion to other anaerobic or facultative bacteria.


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