Refolding chromatography with immobilized mini-chaperones

被引：112

作者：

Altamirano, MM

Golbik, R

Zahn, R

Buckle, AM

Fersht, AR

机构：

[1] UNIV CAMBRIDGE,CTR MRC,CAMBRIDGE CTR PROT ENGN,CAMBRIDGE CB2 2QH,ENGLAND

[2] NATL AUTONOMOUS UNIV MEXICO,FAC MED,DEPT BIOQUIM,MEXICO CITY 04510,DF,MEXICO

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1997年 / 94卷 / 08期

关键词：

protein; renaturation; folding; GroEL; hsp60;

D O I：

10.1073/pnas.94.8.3576

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Mini-chaperones (e.g., a peptide consisting of residues 191-345 of GroEL) that are immobilized on agarose have very efficient chaperoning activity with several proteins that are otherwise recalcitrant to renaturation by conventional methods. We have used immobilized mini-chaperones both in column chromatography and batchwise to renature an insoluble protein from an inclusion body, to refold apparently irreversibly denatured proteins, and to recondition enzymes that have lost activity on storage. Refolding chromatography offers an efficient and simple means to renature proteins in high yield and with biological activity.

引用

页码：3576 / 3578

页数：3

共 15 条

[1] SECONDARY STRUCTURE OF ESCHERICHIA-COLI GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM AMINO-ACID-SEQUENCE AND CIRCULAR-DICHROISM SPECTROSCOPY [J].