Biological control of Bactocera oleae (Diptera: Tephritidae) using a Greek Bacillus thuringiensis isolate.

Bacillus thuringiensis, isolate 114A, was used in toxicity experiments against the wild population ofthe olive pest Bactroceria oleae (Gmelin). In laboratory experiments, spores and crystals of the B.t.

Correlation of the insecticidal activity of the Bacillus thuringiensis A4 strain against Bactrocera oleae (Diptera) with the 140-kDa crystal polypeptide.

The crystals of the soil-isolated Bacillus thuringiensis (Bt) strain A4 consist of two polypeptides with molecular mass of 140 kDa and 32 kDa that exhibit insecticidal activity against adult flies of Bactrocera oleae (Diptera). Plasmid curing applied to this strain resulted in the isolation of several subclones exhibiting alterations in their crystal polypeptides as well as two acrystalliferous subclones. The crystals of subclone 1.

Insecticidal activity of strains of Bacillus thuringiensis on larvae and adults of Bactrocera oleae Gmelin (Dipt. Tephritidae).

The olive fly, Bactrocera oleae, is the key pest on olives in the Mediterranean area. The pest can destroy, in some cases, up to 70% of the olive production. Its control relies mainly on chemical treatments, sometimes applied by aircraft over vast areas, with their subsequent ecological and toxicological side effects.

Sex hormone binding globulin inhibits strongly the uptake of estradiol by human breast carcinoma cells via a deprivative mechanism.

A controversy exists for many years about the role of sex hormone binding globulin (SHBG) in the uptake of estradiol by the cells. Using the estradiol-sensitive human breast carcinoma cell line MCF-7 and SHBG isolated from human serum by a new method, we observed a strong inhibition of estradiol uptake. The inhibition was higher when the concentration of the hormone was low.

Plasmid patterns of Bacillus thuringiensis strains and isolates.

Bacillus thuringiensis produces crystal proteins which are toxic to several orders of economically important insects and other invertebrates. The genes encoding these toxins reside mainly on plasmids. This report consists of a comparative analysis of the plasmid content of a number of B.