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Results for “Botulinum Antitoxin”

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Human-derived immune globulins for the treatment of botulism.

The need for a human-derived immune globulin to replace the equine antitoxins currently used in the treatment of botulism is well recognized. A small group of individuals who had received multiple immunizations with pentavalent botulinal toxoid were plasmapheresed for the purpose of collecting a botulism-immune plasma of human origin to be fractionated for the production of immune globulin. Human-derived immune globulin will offer the advantage over equine antitoxins of not inducing reactions to foreign protein and of having a prolonged effective half-life.

Animals↗
PubMed1971

Rapid detection and quantitative estimation of type A botulinum toxin by electroimmunodiffusion.

An experimental system is described for the detection and quantitative estimation of type A botulinum toxin by electroimmunodiffusion. The method is shown to be rapid, specific, and quantitative. As little as 14 mouse LD(50) per 0.1 ml of type A toxin was detected within 2 hr. When applied to experimentally contaminated foods such as canned tuna, pumpkin, spinach, green beans, and sausage, the technique detected botulinum toxin rapidly and identified it as to type and quantity. A specific rabbit type A antitoxin was produced for this in vitro system since the equine antitoxin (Center for Disease Control) tested in this experiment was found to be unsuitable.

Animals↗
PubMed1962

Activation phenomenon of Clostridium botulinum type E toxin.

Gerwing, Julia (The University of British Columbia, Vancouver, Canada), Claude E. Dolman, and David A. Arnott. Activation phenomenon of Clostridium botulinum type E toxin. J. Bacteriol. 84:302-306. 1962-Highly purified preparations of both nonactivated and trypsin-activated type E botulinus toxins have been analyzed in an ultracentrifuge. Untreated botulinus type E toxin was found to have a sedimentation constant (S(20,w)) of 5.6 Svedberg units, whereas trypsin-activated toxins would not form a boundary under identical conditions. These and other considerations indicate that the mechanism of tryptic activation involves a fragmentation process whereby more toxic sites become exposed.

Antitoxins↗
PubMed1961

Studies on immunity to toxins of Clostridium botulinum. VII. Purification and detoxification of trypsin-activated type E toxin.

Fiock, Mary A. (Fort Detrick, Frederick, Md.), Allen Yarinsky, and James T. Duff. Studies on immunity to toxins of Clostridium botulinum. VII. Purification and detoxification of trypsin-activated type E toxin. J. Bacteriol. 82:66-71. 1961.-A procedure was described for production, purification, and conversion to toxoid of the Clostridium botulinum type E trypsin-treated toxin. A medium containing 1.5% trypticase, 0.5% yeast extract, 0.075% cysteine hydrochloride, and 1.0% glucose consistently yielded activated culture toxicities of 300,000 mouse intraperitoneal ld(50)/ml. Purification of the toxin was accomplished by precipitation with ammonium sulfate, extraction with calcium chloride, and reprecipitation with ethanol in the cold. The resulting partially purified toxin had a specific activity of 45,000,000 ld(50)/mg nitrogen. Purified toxins were converted to toxoid by incubation with formalin and adsorbed on aluminum phosphate. Good immune responses were obtained to the toxoids in mice, guinea pigs, and rabbits.

Animals↗
PubMed2003

Early antitoxin treatment in wound botulism results in better outcome.

Wound botulism in 7 heroin 'skin poppers' produced ophthalmoplegia and descending paralysis. Rapid recovery occurred in 2 who received the antitoxin within the fourth day of symptom onset. A poor outcome was seen in 4 who received the antitoxin after the eighth day of symptoms and 1 who did not receive the antitoxin. Early antitoxin administration is important in achieving a favorable outcome.

Abscess↗