GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II

FEBS Letters

Bergenhem, Nils¹  Persson, Malin²  Carlsson, Uno² 

[1]Department of Biological Chemistry and Institute of Gerontology, 300 NIB, University of Michigan, Ann Arbor, MI 48109-2007, USA

[2]IFM/Department of Chemistry, Linköping University, Linköping, Sweden

关键词: GroEL;    Human carbonic anhydrase II;    Chaperone;    Refolding;    HCA II;    human carbonic anhydrase II;    HCA IIpwt;    pseudo-wildtype human carbonic anhydrase II;    GuHCl;    guanidine hydrochloride;    ANS;    1-anilino-8-naphatalenesulfonic acid;    MBP;    maltose binding protein;   

DOI  :  10.1016/S0014-5793(97)00663-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The kinetics of the refolding of the enzyme, human carbonic anhydrase II (HCA II), at different temperatures, together with the Escherichia coli chaperonin GroEL, has been studied. The Arrhenius plots for the spontaneous, GroEL-assisted, and GroEL/ES-assisted refolding of HCA II show that the apparent activation energy (E _a) is lower in the presence of the chaperonin GroEL alone than for the spontaneous reaction, whereas the apparent activation energy for the GroEL/ES-assisted reaction is almost the same as for the spontaneous reaction (85, 46, and 72 kJ/mol, for the spontaneous, GroEL, and GroEL/ES-assisted reactions, respectively).

【 授权许可】

Unknown