A Toxic Fragment from the Entomocidal Crystal Protein of Bacillus thuringiensis
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概要
- 論文の詳細を見る
Purified crystal protein from Bacillus thuringiensis subsp. dendrolimus strain T84A1gave a single polypeptide band (apparent mol. wt 145, 000) on SDS-PAGEand the only N-terminal amino acid sequence was Met-Asp-Asn-Asn-Pro-Asn-Ile-. No pentose or hexose was detected. Solid phase tryptic digestion of the solubilized crystal protein bound on a DEAE-cellulose column was found to be a successful method to prepare a toxic fragment without denaturation. The resulting fragment (fragment T) was slightly basic (pI 8.9) and the molecular weight was estimated as 58, 000 on SDS-PAGEand by gel filtration without denaturing agents. The apparent number of the amono acid residues was 516 and the N- and C-terminal sequences were determined as Ile-Glu-X-Gly- Tyr-Thr- and -Leu-Arg, respectively. The molar specific toxicities of the solubilized crystal protein and fragment T were nearly identical. The fragment T retained the full toxicity and selectivity of the intact crystal protein. Location of the fragment T in the crystal protein is also discussed.
- 社団法人 日本農芸化学会の論文
著者
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Nagamatsu Yasunori
Department Of Applied Biochemistry Faculty Of Applied Biological Science Hiroshima University
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Hatanaka Chitoshi
Department Of Applied Biochemistry Faculty Of Applied Biological Science Hiroshima University
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HAYASHI Katsuya
Department of Agricultural Chemistry, Faculty of Agriculture, Kyushu University
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ITAI Yuichi
Department of Applied Biochemistry, Faculty of Applied Biological Science, Hiroshima University
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FUNATSU Gunki
Department of Agricultural Chemistry, Faculty of Agriculture, Kyushu University
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