SEPARATION OF TETANUS TOXIN AND TOXOID PROTEINS BY SEPHADEX GEL
- 1 August 1967
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 13 (8) , 1021-1025
- https://doi.org/10.1139/m67-136
Abstract
Tetanus toxin can be fractionated on Sephadex into a non-flocculating protein of over 200,000 molecular weight and a main flocculating fraction with molecular weight under 100,000. After detoxifying, the molecular weight of the main fraction is over 100,000 but under 200,000. A second, slowly flocculating, small fraction appears which is highly antigenic and is possibly a polymer of the main fraction. Both the toxin and toxoid contain a non-flocculating protein with a molecular weight of over 200,000 but which is low in the protective antigen factor. The purity of the main flocculating portion of the toxoid may be increased by removing this fraction.This publication has 2 references indexed in Scilit:
- SEPARATION OF DIPHTHERIA TOXIN PROTEINS BY SEPHADEX GELCanadian Journal of Microbiology, 1966