Abstract
A procedure is described in which the protein crystals produced by Bacillus thuringiensis var. israelensis were solubilized in 50 mM NaOH with 10 mM EDTA at pH 11.7. This solubilization procedure gave protein gel profiles identical with those for intact crystals while maintaining full biological activity in the form of erythrocyte lysis capability. Crystals with and without protease activity were equally toxic to Aedes aegypti larvae.
Original language | English (US) |
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Pages (from-to) | 39-42 |
Number of pages | 4 |
Journal | FEMS Microbiology Letters |
Volume | 21 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1984 |
Keywords
- Aedes aegypti larvae
- Bacillus thuringiensis var. israelensis
- crystal solubilization
- hemolysis
- metalloprotease
- mosquito toxin
ASJC Scopus subject areas
- Microbiology
- Molecular Biology
- Genetics