Abstract: Based on the special physical characteristics of an egg recognition kairomone protein of Telenomus theophilae, a simple, practical, and effective technique (temperature approach) was used to purify the kairomone proteins from Bombyx mori and Theophila mandarina. The compositions of amino acids in kairomone proteins of female accessory glands were very similar between the two moths. Molar percentages of glycine, glutamic and aspartic acid of 15 amino acids detected exceeded 10% in both moths: 28.1%, 18.5% and 12.6%, respectively, in B. mori, and 24.4%, 18.1%, and 10.1%, respectively, in T. mandarina. The total amount of these three amino acids exceeded 50% in both moths. Hydrolyzed by chymotrypsin, the polypeptides of the B. mori kairomone protein formed a waterinsoluble precipitate. The molecular weight of the polypeptides was about 10 kD as judged by SDS-PAGE. This result suggests that the primary structures of the kairomone protein and silk protein from B. mori are similar, both containing a crystalline (precipitate) and a amorphous (supernatant) region.

Key words: Theophila mandarina, Bombyx mori, Telenomus theophilae, kairomone, isolation, amino acid composition