Literature summary for 2.3.3.1 extracted from

Mishra, R.; Seckler, R.; Bhat, R.
Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: how well are protein folding and stability aspects coupled? (2005), J. Biol. Chem., 280, 15553-15560.

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
study on the mechanism of aggregation during refolding of enzyme and its prevention using cosolvent additives of the polyol series. No parallel correlation between the folding effect and the general stabilization is observed. Glycerol is most effective in enhancing the refolding yield of citrate synthase, and a complete recovery of enzymatic activity is observed at 7 M glycerol and 0.01 mg per ml protein. Kinetic experiments suggest that polyols act very early in the refolding process. Both the thermodynamic and the kinetic aspects are critical in the folding process	Sus scrofa

Renatured (Comment)

Organism

study on the mechanism of aggregation during refolding of enzyme and its prevention using cosolvent additives of the polyol series. No parallel correlation between the folding effect and the general stabilization is observed. Glycerol is most effective in enhancing the refolding yield of citrate synthase, and a complete recovery of enzymatic activity is observed at 7 M glycerol and 0.01 mg per ml protein. Kinetic experiments suggest that polyols act very early in the refolding process. Both the thermodynamic and the kinetic aspects are critical in the folding process

Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-

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Release 2023.1 (January 2023)