AN IMMUNOLOGICAL PURIFICATION OF TYPHUS RICKETTSIAE

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Abstract
Rickettsial suspensions prepared from infected yolk sacs and purified by treatment with celite and albumin were found to have esterase, adenosine triphos-phatase, and catalase activities as well as the ability to oxidize glutamate. Treatment of these suspensions with serum prepared by the immunization of rabbits with uninfected yolk sac resulted in agglutination of a small portion of the protein in the suspensions. This agglutination removed the bulk of the esterase, adenosine triphosphatase, and catalase activities but only a fraction of the activity towards glutamate. It is concluded that the enzyme activities other than that towards glutamate are not of rickettsial origin but are due to contamination of the rickettsiae with small amounts of enzymatically highly active host material. The observation that suspensions of rickettsiae which had been adapted to and cultivated in mouse lungs oxidize glutamate provides confirmation that the ability to oxidize glutamate is a characteristic property of rickettsiae.