The toxin activity of Pasteurella pestis cells, strain "Tjiwidej," was found to be associated with two proteins. Using a disc electrophoresis technique in conjunction with mouse lethality, two toxic proteins were isolated exhibiting intraperitoneal LD50's of less than 1.0 to 1.5 µg protein. Each produced a single characteristic precipitin band on agar gel diffusion plates. The slower migrating toxin in gel diffusion or disc electrophoresis was designated as toxin A. It was shown to be sensitive to deoxycholate and digitonin, did not accumulate in 5-fluorotryptophan treated cells, and was associated with the membrane fraction of the cell. The faster migrating toxin B, apparently is resistant to surface-active agents, and is not affected by treatment of cells with 5-fluorotryptophan. Toxin B is associated with the soluble or cytoplasmic fraction of the cell. This evidence suggested that each toxin represented a distinctly different molecular species. The possibility is discussed that toxin B is synonymous with the murine toxin previously isolated by paper curtain electrophoresis which revealed only one antigen band in the Oudin precipitin reaction.
THE IDENTIFICATION AND ISOLATION OF TWO MOUSE-TOXIC PROTEIN COMPONENTS IN EXTRACTS FROM PASTEURELLA PESTIS
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Thomas C. Montie, Diane B. Montie, Samuel J. Ajl; THE IDENTIFICATION AND ISOLATION OF TWO MOUSE-TOXIC PROTEIN COMPONENTS IN EXTRACTS FROM PASTEURELLA PESTIS . J Exp Med 1 December 1964; 120 (6): 1201–1213. doi: https://doi.org/10.1084/jem.120.6.1201
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