The ferredoxin/thioredoxin system of enzyme regulation in a cyanobacterium |
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| Authors: | B. C. Yee A. de la Torre N. A. Crawford C. Lara D. E. Carlson B. B. Buchanan |
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| Affiliation: | (1) Institute of Microbiology, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland;(2) Mikrobiologisches Institut der ETH, CH-8092 Zürich |
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| Abstract: | 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 pH 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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| Keywords: | Bacillus thuringiensis Protein crystal Solubilization Subumts MW determination Biological activity |
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