IMMUNOGENICITY OF HIGHLY PURIFIED ^|^alpha;-TOXOID OF CLOSTRIDIUM PERFRINGENS
نویسندگان
چکیده
منابع مشابه
Highly conserved alpha-toxin sequences of avian isolates of Clostridium perfringens.
Clostridium perfringens causes necrotic enteritis in chickens, and alpha-toxin has been suggested to be a key virulence determinant. Analysis of the alpha-toxin of 25 chicken-derived C. perfringens strains demonstrated high homology to mammal-derived strains rather than to the only avian-derived C. perfringens alpha-toxin sequence reported previously.
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A potent toxin was produced by a strain of Clostridium perfringens PB6K in a chemically defined medium consisting of 19 amino acids, fructose, vitamins and minerals. A large amount of L-arginine (10 mg/ml or higher concentration) was required for toxin production. An excess of L-cystine (0.1 mg/ml or higher) reduced the yield of toxin seriously. Zinc and manganese, though ineffective for growth...
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Clostridium perfringens alpha-toxin is a key mediator of gas gangrene, which is a life-threatening infection that manifests as fever, pain, edema, myonecrosis, and gas production. Alpha-toxin possesses phospholipase C and sphingomyelinase activities. The toxin is composed of an N-terminal domain (1-250 aa, N-domain), which is the catalytic site, and a C-terminal domain (251-370 aa, C-domain), w...
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Recombinant Bacillus subtilis endospores have been used to vaccinate against tetanus and anthrax. In this work, we have developed spores that could be used to vaccinate against Clostridium perfringens alpha toxin and that could be used to protect against gas gangrene in humans and necrotic enteritis in poultry. The primary active agent in both cases is alpha toxin. A carboxy-terminal segment of...
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Exo-alpha-N-acetylgalactosaminidase has been purified 8000-fold from Clostridium perfringens by gel filtration, ion exchange chromatography, isoelectric precipitation, and negative adsorption on human O type erythrocytes. The resulting enzyme is active at physiological pH and temperature. Phenyl glycosides, oligosaccharides, mucins, glycolipids, and cell membranes are substrates for this enzyme...
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ژورنال
عنوان ژورنال: Japanese Journal of Medical Science and Biology
سال: 1972
ISSN: 0021-5112,1884-2828
DOI: 10.7883/yoken1952.25.53