Investigations have been made on the purification of Clostridium botulinum type E toxin and an attempt made to elucidate the phenomenon of trypsin activation.
Type E botulinus toxin produced in meat infusion medium in dialysis sacs was partially purified by Seitz filtration and ethanol precipitation. Treatment of this toxic preparation with trypsin produced a 20 - 50 fold increase in potency.
Both non-activated and trypsin-activated toxins were further purified by elution through cellulose ion-exchange columns and dried by lyophilization. Refractionation of these dried toxins effected even further purity.
These highly purified preparations of both non-activated and trypsin-activated type E toxin were then analysed in the ultracentrifuge. The former was found to have a sedimentation constant of 5.6 Svedburg units whereas activated toxin did not form a boundary under identical conditions.
Together with other considerations, this evidence indicates that the activation mechanism involves a fragmentation process whereby more toxic sites become exposed on the toxin molecule. / Science, Faculty of / Microbiology and Immunology, Department of / Graduate
| Identifer | oai:union.ndltd.org:UBC/oai:circle.library.ubc.ca:2429/39013 |
| Date | January 1962 |
| Creators | Arnott, David Alexander |
| Publisher | University of British Columbia |
| Source Sets | University of British Columbia |
| Language | English |
| Detected Language | English |
| Type | Text, Thesis/Dissertation |
| Rights | For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use. |
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