FEMS Microbiology Letters · 1986 · 67 citations · 14 references
Life SciencesBiologyEntomologyInsect MorphologyInsect ToxicologyParasitologyComparative ParasitologyLarval MorphologyMosquito BiologyParasitoid BiologyMosquito AnatomyMosquito ProteomicsMosquitocidal BioassaysPolyacrylamide Gel ElectrophoresisSodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis
The mosquitocidal parasporal bodies of the PG-14 isolate of Bacillus thuringiensis ssp. morrisoni and B. thuringiensis ssp. israelensis were purified on sodium bromide gradients and compared using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) electron microscopy and bioassays against mosquito larvae. The parasporal bodies of both subspecies were spherical/ovoidal, approx. 0.7–1.2 μm in diameter, and contained major proteins of 28, 65, 126 and 135 kDa. In addition to these, the parasporal body of B. thuringiensis ssp. morrisoni contained at least one other major protein, of 144 kDa, which correlated with the presence of a quasi-bi-pyramidal inclusion not present in the B. thuringiensis ssp. israelensis parasporal body. The LC50 for parasporal bodies of each subspecies was in the range of 3 ng/ml for fourth-instars of Aedes aegypti. These results indicate that B. thuringiensis Serotype 8a:8b, which is generally considered to produce proteins toxic to lepidopterous insects, is capable of producing a protein toxin complement similar to B. thuringiensis Serotype 14.
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Maturation of the head of bacteriophage T4
Ulrich K. Laemmli, Manuel Favre · Journal of Molecular Biology · 1973 · 3.7K citations
The biology of Aedes albopictus.
PubMed · 1985 · 907 citations