The procedure for isolation and purification of Pasteurella multocida serovariant D toxin has been described. It includes the three steps of protein precipitation from cultural filtrates by 70% ammonium sulfate, chromatography of the concentrated material on Ultragel AcA44 gel-filtration on Sephracryl S-200. The proposed technique permits one the 155-fold purification of the preparation with 32.6% yield estimated by biological activity. The obtained purified preparation is homogeneous in polyacrylamide gel electrophoresis. The immunological methods also confirm the homogeneity of the preparation. The minimal dermonecrotic dose for guinea pigs of the purified 120 kDa toxin is 78 ng and LD50 for mice is 280 ng. Pasteurella multocida toxin is found to be a thermolabile protein sensitive to trypsin, glutaraldehyde and formaldehyde treatments.
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