NDLI: Specific Toxicity of Î´-Endotoxins from Bacillus thuringiensis to Bombyx mori.

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Multifunctional Flow-injection Biosensor for the Simultaneous Measurement of Creatinine, Glucose, and Urea.

Specific Toxicity of Î´-Endotoxins from Bacillus thuringiensis to Bombyx mori.

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Purification and Characterization of an Adipamidase from a Mutant Strain of Brevibacterium sp. Involved in Dinitrile Degradation.

Purification and Properties of Aldehyde Reductases from Yeasts That Convert Ethyl 2-Acetamido-3-oxobutyrate to Optically Active Ethyl 2-Acetamido-3-hydroxybutyrate.

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Ethanolysis of Substituted 2-Ethoxy-1,3,2-oxazaphospholidine and -thiazaphospholidine Oxides Monitored by (31)P-NMR as a Model for Interaction with Acetylcholinesterase.

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Reactions Catalyzed by Cycloinulo-oligosaccharide Fructanotransferase.

Basidifferquinone Analogues, Basidifferquinone B and C, Which Induce Fruiting-body Formation of a Basidiomycete, Favolus arcularius.

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Effect of the Quantity and Nutritional Quality of Dietary Proteins on the Transcriptional Activity of Insulin-like Growth Factor-I and Insulin-like Growth Factor Binding Protein-1 Genes.

Effects of Orally Administered Bovine Lactoferrin on the Faecal Enterobacteriaceae of SPF Mice Fed Milk.

Year: 1993 Volume: 57 Issue: 1

Year: 1992 Volume: 56

Specific Toxicity of Î´-Endotoxins from Bacillus thuringiensis to Bombyx mori.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ihara, H. Kuroda, E. Wadano, A. Himeno, M.
Description	Country affiliation: Japan Author Affiliation: Ihara H ( a Department of Agricultural Chemistry, College of Agriculture , University of Osaka Prefecture , Sakai, Osaka 591 , Japan.); Kuroda E ( a Department of Agricultural Chemistry, College of Agriculture , University of Osaka Prefecture , Sakai, Osaka 591 , Japan.); Wadano A ( a Department of Agricultural Chemistry, College of Agriculture , University of Osaka Prefecture , Sakai, Osaka 591 , Japan.); Himeno M ( a Department of Agricultural Chemistry, College of Agriculture , University of Osaka Prefecture , Sakai, Osaka 591 , Japan.)
Abstract	Two Î´-endotoxins, CryIA(a) and CryIA(b), from Bacillus thuringiensis subsp.. aizawai were used to investigate the specificity in insecticidal activity. CryIA(a) was 17-fold more toxic to Bomhyx mori than CryIA(b). After in vitro solubilization and digestion of these Î´-endotoxins, the specificity of toxicity was retained. Trypsin-activated CryIA(a) and CryIA(b) showed specific, high affinity and saturable binding to brush border membrane vesicles (BBMV) from B. mori midguts. These two toxins competed for the same binding site. Dissociation constant for CryIA(a) and CryIA(b) binding to B. mori BBMV was O.89nM and 1.46 nM, respectively. In both toxins, dissociation reaction followed a biphasic process with a fast and a very slow component, suggesting that binding of the toxins proceeds through a reversible component and an apparently irreversible component. In the CryIA(a) dissociation reaction, the irreversible component comprised a large portion of total binding. On the other hand in that of CryIA(b), the reversible component was major. These results suggest that the specific toxicity of the toxins to B. mori may depend mainly on irreversibility.
File Format	HTM / HTML
ISSN	09168451
e-ISSN	13476947
Journal	Bioscience, Biotechnology, and Biochemistry
Issue Number	2
Volume Number	57
Language	English
Publisher	Taylor & Francis
Publisher Date	1993-01-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Discipline Biotechnology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Medicine Analytical Chemistry Molecular Biology Biochemistry Applied Microbiology and Biotechnology Biotechnology

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