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Insecticidal protein

McBride, K.E. et al. (1995). Amphfication of a chimeric Bacillus gene in chloroplasts leads to an extraordinary level of an insecticidal protein in tobacco. Biotechnology (NY) 13 362-365. [Pg.75]

It has already been pointed out that many naturally occurring insect-specific toxins are proteins. This means that the genes coding for those proteins can be isolated and introduced into crop plants, driven by selected promoters that allow the insecticidal proteins to be produced... [Pg.70]

Haas, G.J. and E.J. Guardia. 1968. Production of antibodies against insecticide-protein conjugates. Proc. Soc. Exp. Biol. Med. 129 546-551. [Pg.178]

The bacterium Bacillus thuringiensis forms an internal crystal that contains a number of insecticidal protein toxins. When eaten by the insect, the crystal dissolves in the midgut, the toxin mixture is released, and the proteins are cleaved into active forms. The toxins bind specifically to midgut cells and assemble a pore that leads to disintegration of the cells, gut paralysis, and death. B. thuringiensis strains have toxins specific for caterpillars, beetles, or flies. They have little or no effect on mammals. [Pg.240]

Stotzky, G. (2000). Persistence and biological activity in soil of insecticidal proteins from Bacillus thuringiensis and of bacterial DNA bound on clays and humic acids. Journal of Environmental Quality, 29, 691-705. [Pg.265]

The report by Haas and Guardia (18) pertains to their efforts to apply immunological methods for the assay of pesticide residues, and expresses their aim to test the suitability of methods for field analytical purposes. Haas and Guardia also used DDT and malathion to represent two of the most important classes of insecticides, chlorinated hydrocarbons and organophosphorus compounds. They first attempted to prepare insecticide-protein antigens in which enzymes were used as the protein carrier. Antiserum of rabbits injected with DDA-carbonic anhydrase or malathion-chymotrypsin failed to show the presence of the respective antibodies. [Pg.168]

B.t. insecticidal protein 46% TSP Tobacco leaves [19] Highest protein in transgenic plant to date... [Pg.2491]

Although inclusion bodies are generally amo hous, expression of insecticidal proteins in E, coli has been shown to result in the formation of crystalline, bipyramidal inclusion bodies in the cytoplasm when the cells were grown at 30°C (65). Growth at at 37 C induced the production of amorphous, spherical structures. The foreign protein corresponded to 70% of the total protein of these aggregates compared to 9()% in the bipyramidal inclusion bodies formed at 30 C. [Pg.9]

Commercial preparations of B.t.. obtained through conventional fermentation techniques, have been used for more than two decades as biological insecticides (I). They exhibit desirable properties such as high insect toxicity and environmental safety. B.t. does not affect non-target insects and is completely nontoxic to vertebrates. Nevertheless its use has been limited due to high production costs, limited stability in field conditions and a too narrow insecticidal spectrum. The insecticidal activity of B.t. relies in the crystalline inclusions which are produced upon sporulation. The crystals contain insecticidal proteins, delta-endotoxins, which affect the midgut epithelium of sensitive insects. The exact mechanism of their toxic activity is still unknown. [Pg.274]

Quantitative immunological analysis indicated that the insecticidal protein toxin constituted approximately 1% of the total protein in 112-12RN and Ps3732RN when the B.t. gene was in the same orientation as the Km gene. Placement of the B.t. gene in the opposite orientation to the Km gene resulted in lower levels of protein production, estimated to constitute 0.1% of the total protein of the cell. [Pg.283]

A new class of insecticidal toxins called vegetative insecticidal proteins has recently been isolated from Bt. They are produced during the vegetative growth stage. The proteins are different from other known proteins, and their function and versatility for insect control have yet to be elucidated. [Pg.68]

Although historically most useful antibiotics have come from spore forming microorganisms, marine organisms have yielded the candidate antitumor peptide didemnin B [77327-50-0] (2) and cytostatic peptides such as the patellamides (3). Many of the marine peptides have little or no antimicrobial activity. Antibacterial peptides called magainins are found in frog skin (4) and antibacterial proteins called defensins are found in mammalian white blood cells (5). The commercially important insecticidal proteins from Bacillus thuringensis (6) are not discussed herein nor are the numerous peptide siderophores (7,8), which, except for the albomycins (9), are usually not antimicrobial. [Pg.146]

Bt and from conventional insecticides. As avidin is a natural food protein found in eggs, it may be easier to register than other insecticide proteins that are not present in the food supply [352]. Beta-glucuro-nidase was also produced in corn seed by ProdiGene for use as a diagnostic enzyme, but it is not commercially available [285, 286]. [Pg.853]


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Bacillus thuringiensis, insecticidal crystal proteins

Dipteran-specific insecticidal crystal proteins

Encoding insecticidal proteins

Insecticidal 6-endotoxin proteins

Vegetative insecticidal proteins

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