The subunits of the parasporal crystal ofBacillus thuringiensis: Size, linkage and toxicity
✍ Scribed by Hans E. Huber; Peter Lüthy; Hans-Rudolf Ebersold; Jean-Louis Cordier
- Publisher
- Springer
- Year
- 1981
- Tongue
- English
- Weight
- 837 KB
- Volume
- 129
- Category
- Article
- ISSN
- 0302-8933
No coin nor oath required. For personal study only.
✦ Synopsis
The solubility properties and the number of disulfide groups per molecule of the crystal protein of Bacillus thuringiensis were shown to be similar to that of wool keratin. Dissolution of the crystals required scission of S-S bonds. This could be achieved at neutral p H without loss of toxicity. Molecular weight determinations with gel electrophoresis and ultracentrifugation indicated that the crystal subunit is a dimer. With the exception of the variety israelensis, all strains belonging to ten different subspecies revealed crystal subunits of the same molecular weight.
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