mfe_38_1-2_097_100.pdf 1.22 MB
Bacillus thuringiensis subsp. coreanensis A2316 is a newly isolated strain from Yonakunijima Island in Japan. It produces the proteinaceous inclusion body (crystal) which has no insecticidal and hemolytic activities. When the crystal proteins were digested by proteinase K, they exhibited the strong cytotoxicity against human leukemic T cell, MOLT-4. The proteinase K-digested A2316 crystal proteins have little damage upon the cell membrane of MOLT-4, suggesting that the cell death of MOLT-4 was induced through a mechanism other than the colloid-osmotic swelling and cell lysis as caused by hitherto known B. thuringiensis crystal proteins. The 29-kDa polypeptide proved to be an active component of the proteinase K-digested A2316 crystal proteins. EC(50) of the purified 29-kDa polypeptide was 0.0579 μg/ml. The N-terminal amino acid sequence of the 29-kDa polypeptide was identical with that of p29 produced by B. thuringiensis A1519 strain and shared no significant homology with all the known proteins, suggesting that this polypeptide belong to a new family of B. thuringiensis crystal proteins.
Memoirs of the Faculty of Engineering, Okayama University
Faculty of Engineering, Okayama University
Departmental Bulletin Paper
|Eprints Journal Name||