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Publication Information

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Title: The biochemistry of the protein crystal toxin of Bacillus thuringiensis

Author: Fast, Paul G.;

Date: 1985

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)

   Note: This article is part of a larger document. View the larger document

Description: The 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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Fast, 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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