Significance of 12S toxin of Clostridium botulinum type E.
- 1 June 1969
- journal article
- Vol. 98 (3) , 1173-8
Abstract
The pathogenesis of type E botulism is discussed as an aspect of the physicochemical and biological properties of 12S toxins (prototoxin and trypsin-activated 12S toxin) and the Ealpha and Ebeta components of each 12S toxin. A molecular weight of 350,000 was determined for each 12S toxin and 150,000 for Ealpha and Ebeta. Owing to the structure comprising the subunits Ealpha and Ebeta, 12S toxins are much more stable than Ealpha at low pH values and high temperatures. Such was also the case with type A 19S toxin and its alpha component. The Ealpha component alone accounts for the total toxicity of type E toxin. The toxic substance detected in the blood of the animals administered 12S toxins orally or parenterally was identified as Ealpha from the molecular size and the chromatographic pattern. Prototoxin escaping from detoxification in the stomach owing to the subunit structure may undergo dissociation in the intestine to release the Ealpha component. After absorption, the activated Ealpha appeared in the circulating blood without any further signs of dissociation or enzymatic digestion.This publication has 13 references indexed in Scilit:
- Purification and some properties of Clostridium botulinum type-E toxinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- Isolation of chromatographically pure toxin of Clostridiumbotulinum type BBiochemical and Biophysical Research Communications, 1968
- Dissociation of Clostridium,botulinum type-E toxinBiochemical and Biophysical Research Communications, 1967
- Chromatographic fractionation of the crystalline toxin of Clostridiumbotulinum type aBiochemical and Biophysical Research Communications, 1966
- Low molecular weight forms of type A botulinum toxin. II. Action of pepsin on intact and dissociated toxinArchives of Biochemistry and Biophysics, 1963
- ON THE SIZE OF THE TOXIC PARTICLE PASSING THE INTESTINAL BARRIER IN BOTULISMThe Journal of Experimental Medicine, 1960
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951