Toxicity and composition of protease-inhibited Bacillus thuringiensis var. israelensis crystals

Mary Ann Pfannenstiel, Elise J. Ross, Vance C. Kramer, Kenneth W. Nickerson

Research output: Contribution to journalArticle

29 Scopus citations


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 languageEnglish (US)
Pages (from-to)39-42
Number of pages4
JournalFEMS Microbiology Letters
Issue number1
Publication statusPublished - Jan 1984



  • Aedes aegypti larvae
  • Bacillus thuringiensis var. israelensis
  • crystal solubilization
  • hemolysis
  • metalloprotease
  • mosquito toxin

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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