@article{mbs:/content/journal/micro/10.1099/00221287-135-11-3109, author = "Ryu, Sangryeol and Labbe, Ronald G.", title = "Coat and Enterotoxin-related Proteins in Clostridium perfringens Spores", journal= "Microbiology", year = "1989", volume = "135", number = "11", pages = "3109-3118", doi = "https://doi.org/10.1099/00221287-135-11-3109", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-135-11-3109", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Coat proteins from mature spores of two enterotoxin-positive (Ent+) and two enterotoxin-negative (Ent+) strains of Clostridium perfringens were solubilized using 50 mm-dithiothreitol and 1% sodium dodecyl sulphate at pH 9·7, and alkylated using 110 mm-iodoacetamide to prevent aggregation. The coat proteins and C. perfringens type A enterotoxin (CPE) were separated by SDS-PAGE and analysed by Western blotting using anti-CPE antibody. As previously reported, CPE aggregated in the presence of SDS, but no aggregation occurred at concentrations below 15 μg CPE ml−. Two CPE-related proteins (34 and 48 kDa) were found in the solubilized spore coat protein of Ent+ strains while only the 48 kDa CPE-related protein was found in the spore coat fraction of Ent+ strains. CPE-related proteins comprised 2·7% and 0·8% of the total solubilized coat protein of Ent+ and Ent+ strains respectively. CPE-related proteins could be extracted from the spores with 1 % SDS alone. They could also be released by disruption of whole spores, indicating that the CPE-related proteins may be in the spore core or trapped between the core and coat layers. The results suggest that CPE is not a major structural component of the coat fraction of C. perfringens spores.", }