Axial filaments of Treponema hyodysenteriae were purified and examined by transmission electron microscopy. The size and fine structure of the filaments were similar to those of Treponema zuelzerae and Treponema phagedenis biotype reiterii. Filaments were dissociated by heat and 2-mercaptoethanol and examined by polyacrylamide-gel electrophoresis. Six protein bands were evident, with approximate molecular weights of 39,000, 29,000, 27,000, 22,000, 21,000, and 18,500 daltons. All the proteins reacted with T hyodysenteriae and T innocens rabbit antisera, using the immunoblot technique.
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