Some properties of beta-toxin produced by Clostridium perfringens type C
- 1 August 1978
- journal article
- research article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 21 (2) , 678-680
- https://doi.org/10.1128/iai.21.2.678-680.1978
Abstract
Purified .beta.-toxin from C. perfringens type C was a single polypeptide chain protein with a MW of approximately 30,000. The toxin was heat labile, with 75% of its activity being inactivated by incubation at 50.degree. C for 5 min. Biological activity of the purified toxin was completely destroyed on exposure to trypsin for 30 min at 37.degree. C. The 50% lethal dose for mice was 1.87 .mu.g of purified toxin.This publication has 7 references indexed in Scilit:
- Purification of phospholipase C (alpha-toxin) from Clostridium perfringensBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- [Preliminary data on the purification and structure of Clostridium perfringens alpha-toxin].1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Cereolysin: Production, Purification and Partial CharacterizationJournal of General Microbiology, 1967
- EFFECT OF pH ON TOXINOGENESIS BY CLOSTRIDIUM PERFRINGENS TYPE CCanadian Journal of Microbiology, 1964
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964