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The subunits of the parasporal crystal of Bacillus thuringiensis: Size, linkage and toxicity (1981)

Huber, Hans E. ; Lüthy, Peter ; Ebersold, Hans-Rudolf ; [et al.]

Springer

Archives of microbiology 129 (1981), S. 14-18

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ISSN: 1432-072X

Keywords: Bacillus thuringiensis ; Protein crystal ; Solubilization ; Subumts ; MW determination ; Biological activity

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00417171

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