Purification and characterization of the active fragment from Bacillus thuringiensis delta-toxin |
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| Authors: | S Tyski Y Fujii C Y Lai |
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| Affiliation: | 1. Bacterial Toxin Research Innovation Laboratory, Institute of Molecular Biosciences, Mahidol University, Salaya Campus, Nakornpathom, 73170, Thailand;2. Division of Health and Applied Sciences, Biochemistry Graduate Program, Faculty of Science, Prince of Songkla University, Hatyai, Songkhla, 90110, Thailand;3. Biophysics Institute for Research and Development (BIRD), Chiang Mai, 50110, Thailand;4. Department of Biochemistry, School of Medicine, Tzu Chi University, Hualien, 97004, Taiwan;5. Graduate Program in Immunology, Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, 10700, Thailand;1. Graduate School of Science and Technology, Kwansei Gakuin University, 1 Gakuen Uegahara, Sanda, Hyogo, 669‐1330, Japan;2. Department of Veterinary Anatomy, School of Veterinary Medicine, Tottori University, 4-101 Koyama Minami, Tottori, Tottori, 680-8553, Japan;3. Department of Anatomy, School of Medicine, Aichi Medical University, 1-1 Yazakokarimata, Nagakute, Aichi, 480-1195, Japan;4. Department of Pathology and Laboratory Medicine, University of Rochester, 601 Elmwood Ave, Rochester, NY, 14642, USA;5. Department of Biomedical Sciences, School of Biological and Environmental Sciences, Kwansei Gakuin University, 1 Gakuen Uegahara, Sanda, Hyogo, 669‐1330, Japan;1. Department of Basic Medical Sciences, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, 156-8506, Japan;2. Graduate School of Medical and Dental Sciences, Niigata University, Niigata-shi, Niigata, 951-8510, Japan;3. Center for Basic Technology Research, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, 156-8506, Japan |
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| Abstract: | Limited tryptic hydrolysis of a partially purified delta-toxin (Mr = 100,000) from Bacillus thuringiensis, has produced a polypeptide fragment of Mr = 60,000 containing the full biological activity. The fragment was the only polypeptide observed in the polyacrylamide-gel electrophoresis of the delta-toxin after treatment with trypsin and could be purified by DEAE-cellulose chromatography. Amino acid and partial sequence analyses indicate that the 60,000 Mr fragment has been derived from the mid-section of the holotoxin peptide; over 80% of Lys, 65% of Pro and 50% of His residues in the holotoxin have been lost in the active fragment. This section must contain the active site since its specific insecticidal activity is approximately twice that of the holotoxin. The active fragment shows complete cross-reactivity with the antiserum raised against the native toxin, and appeared to possess higher thermal stability than the mother protein. It provides a powerful tool for studies of the structure involved in the insecticidal activity. |
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