Abstract
The crystal protein of Bacillus thuringiensis var. tolworthi has been separated into two polypeptide chains having molecular weights of 55000 (A) and 120000 (B). The ratio of A to B in the crystal appears to be 2:1 on a molar basis. Differences in amino‐acid composition and biological activity exclude the possibility that the larger polypeptide chain is a dimer of the smaller one. The full toxicity of the unfractionated protein to larvae of Pieris brassicae is retained by fraction A, whereas fraction B is non‐toxic.
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