PURIFICATION OF A PROTEIN TOXIN FROM CORYNEBACTERIUM ULCERANS
- 1 November 1980
- journal article
- research article
- Published by Microbiology Society in Journal of Medical Microbiology
- Vol. 13 (4) , 587-592
- https://doi.org/10.1099/00222615-13-4-587
Abstract
Toxin from C. ulcerans strain 378 was purified 66-fold by ammonium sulfate fractionation, dialysis, gel filtration on Ultrogel AcA22, ion-exchange chromatography on DEAE-cellulose and gel filtration on AcA54. On polyacrylamide-gel electrophoresis, the purified material was homogeneous, staining for protein, but not carbohydrate or lipid. The MW of C. ulcerans toxin was 13,000 as determined by SDS(sodium dodecyl sulfate)-polyacrylamide-gel electrophoresis and 15,000 as determined by gel filtration on AcA54.This publication has 3 references indexed in Scilit:
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- Toxin‐producing diphtheria‐like organisms isolated from cases of sore throatThe Journal of Pathology and Bacteriology, 1951
- Starch‐fermenting gelatin‐liquefying corynebacteria isolated from the human nose and throatThe Journal of Pathology and Bacteriology, 1948