作者: H.P. Bietlot , J.P. Schernthaner , R.E. Milne , F.R. Clairmont , R.S. Bhella
DOI: 10.1016/S0021-9258(18)53087-8
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摘要: Toxin generated by activation of the Bacillus thuringiensis CryIA(c) crystal protein (protoxin) with bovine trypsin was separated into two components anion-exchange chromatography. One component (T2) DNA-associated toxin, and other DNA-free toxin (T1). Only one major protoxin observed, it found to be associated DNA. The DNA from T2 varied in size 100 300 base pairs, whereas solubilized contained 20-kilobase as component. DNase treatment converted T1 toxin. In contrast, resistant digestion not dissociated 1.5 M NaCl. appeared elute a complex molecular mass > 2 x 10(6) Da on gel-filtration No after extensive or dissociation succinylation lysine residues. It is proposed that binds COOH-terminal half essential for maintaining conformational integrity required formation generation