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The biochemistry of the protein crystal toxin of Bacillus thuringiensisAuthor(s): Paul G. Fast
Source: In: Grimble, David G.; Lewis, Franklin B., coords. Proceedings, Symposium: Microbial control of spruce budworms and gypsy moths; 1984 April 10-12; Windsor Locks, CT. Gen. Tech. Rep. NE-100. Broomall, PA: U.S. Department of Agriculture, Forest Service, Northeastern Forest Experiment Station. 109-113
Publication Series: General Technical Report (GTR)
Station: Northeastern Research Station
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DescriptionThe crystal consists of dimeric protein subunits. The monomer peptide chains are held together in the subunit and the subunit in the crystal by disulfide and non-covalent bonds. The monomer peptide has a molecular weight of about 130 kdaltons which, in the presence of proteases, is hydrolyzed to a protease-resistant-protein of 65 kda that is toxic both to larvae by injection and to tissue culture cells and thus is the active toxin. The gene for this protein is on a plasmid which greatly simplifies the work of the genetic engineers. The gene has been partially sequenced and the secondary structure of this part has been predicted but not demonstrated.
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CitationFast, Paul G. 1985. The biochemistry of the protein crystal toxin of Bacillus thuringiensis. In: Grimble, David G.; Lewis, Franklin B., coords. Proceedings, Symposium: Microbial control of spruce budworms and gypsy moths; 1984 April 10-12; Windsor Locks, CT. Gen. Tech. Rep. NE-100. Broomall, PA: U.S. Department of Agriculture, Forest Service, Northeastern Forest Experiment Station. 109-113
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