CHAPERONIN 10 Chemische Eigenschaften,Einsatz,Produktion Methoden
Verwenden
Chaperonin 60 from
Escherichia coli has been used:
- in mass spectroscopy
- in cryo-electron microscopy imaging as control for testing particle distribution
- as standard in infrared spectrum measurements
Biochem/physiol Actions
Chaperonin 60 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. In vitro, purified GroEL together with purified GroES in the presence of Mg-ATP facilitate refolding and reactivation of denatured proteins, e.g., the photosynthetic enzyme rubisco and the mitochondrial enzyme rhodanese.The folding activity of a 1:1 molar mixture of GroEL and GroES was tested using urea-denatured rhodanese. At least 2-fold reactivation of rhodanese over the spontaneous reactivation was obtained.
CHAPERONIN 10 Upstream-Materialien And Downstream Produkte
Upstream-Materialien
Downstream Produkte
