Oxidative refolding chromatography:: folding of the scorpion toxin Cn5
Oxidative refolding chromatography:: folding of the scorpion toxin Cn5
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DOI：
10.1038/6192
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发表时间：
1999-02-01
影响因子：
46.9
通讯作者：
Fersht, AR
中科院分区：
文献类型：
--
作者：
Altamirano, MM;García, C;Fersht, AR
We have made an immobilized and reusable molecular chaperone system for oxidative refolding chromatography. Its three components-GroEL minichaperone (191-345), which can prevent protein aggregation; DsbA, which catalyzes the shuffling and oxidative formation of disulfide bonds; and peptidyl-prolyl isomerase-were immobilized on an agarose gel. The gel was applied to the refolding of denatured and reduced scorpion toxin Cn5. The 66-residue toxin, which has four disulfide bridges and a cis peptidyl-proline bond, had not previously been refolded in reasonable yield. We recovered an 87% yield of protein with 100% biological activity.
