Purification of recombinant cholera toxin polypeptide A2 and reconstitution with the cholera toxin B subunit.

被引:0
作者
McCann, JA [1 ]
Picking, WD [1 ]
机构
[1] ST LOUIS UNIV,DEPT BIOL,ST LOUIS,MO 63103
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暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Polypeptide A2 of cholera toxin (CTA2) was cloned, expressed and purified as a fusion protein possessing a leader with six tandem histidine residues. Following affinity purification, recombinant CTA2 was labeled with a fluorescent probe at its single cysteine and reconstituted with the cholera toxin B subunit (CTB) pentamer. This novel CTB/CTA2 complex will be useful for monitoring the position of the site of attachment of the cytotoxic Al polypeptide of cholera toxin relative to sites on CTB or G(M1)-containing membranes.
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页码:39 / 46
页数:8
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