Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES

FEBS Letters

Hartman, Dallas J.¹  Peralta, Dadna¹  Høj, Peter B.¹  Hoogenraad, Nicholas J.¹ 

[1]Department of Biochemistry, La Trobe University, Bundoora, Victoria 3083, Australia

关键词: Malate dehydrogenase;    Aggregation;    Denaturation;    MDH;    malate dehydrogenase;   

DOI  :  10.1016/0014-5793(94)80381-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Pig heart mitochondrial malate dehydrogenase was chemically denatured in guanidine HCl. Upon 50-fold dilution of the denaturant spontaneous refolding could be observed in the temperature range 12–32°C. At 36°C spontaneous refolding was not observed but a stable folding intermediate that is fairly resistant to aggregation was formed. This intermediate is readily refolded by the chaperonins GroEL and GroES and may prove useful in future attempts to describe several aspects of chaperonin action at physiological temperatures.

【 授权许可】

Unknown