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Coat proteins from the spores of Bacillus sphaericus 1593 were separated by preparative polyacrylamide gel electrophoresis. Neutralising antibodies were raised against a single protein band exhibiting toxicity to mosquito larvae. IgG was purified and coupled to CNBr-activated Sepharose 4B to be used as an immunoaffinity matrix. The larvicidal protein was purified to electrophoretic homogeneity using this immunoaffinity column. The single protein species resolved into four peptides of molecular weights 42.6, 44.1, 50.7 and 51.3 KDa on polyacrylamide gel electrophoresis under denaturing conditions. This protein contained 12% carbohydrates. The purified protein exhibited an LC50 value of 8.3 +/- 1.6 ng/ml when tested against early third instar larvae of the mosquito Culex pipiens var quinquefasciatus.
M L Narasu, and
K P Gopinathan
December 1987,
Experimental parasitology,
M L Narasu, and
K P Gopinathan
December 1985,
Indian journal of malariology,
M L Narasu, and
K P Gopinathan
January 1984,
Journal of general microbiology,
M L Narasu, and
K P Gopinathan
October 1983,
Applied and environmental microbiology,
M L Narasu, and
K P Gopinathan
September 1987,
Molecular microbiology,
M L Narasu, and
K P Gopinathan
March 1981,
Experientia,
M L Narasu, and
K P Gopinathan
March 1987,
Biochemical and biophysical research communications,
M L Narasu, and
K P Gopinathan
January 1988,
Annales de l'Institut Pasteur. Microbiology,
M L Narasu, and
K P Gopinathan
June 1980,
Applied and environmental microbiology,
M L Narasu, and
K P Gopinathan
September 1991,
The Indian journal of medical research,
