Protein refolding in predominantly organic media markedly enhanced by common salts
Journal Article
·
· Biotechnology and Bioengineering
- Massachusetts Inst. of Tech., Cambridge, MA (United States). Dept. of Chemistry
The refolding/reoxidation of unfolded/reduced hen egg-white lysozyme was investigated in a variety of predominantly nonaqueous media consisting of protein-dissolving organic solvents and water. It was discovered that LiCl and other common salts dramatically increased the refolding yield of lysozyme in such nonaqueous systems, while reducing it in water. The mechanism of this surprising phenomenon appears to involve salt-induced suppression of nonspecific lysozyme aggregation during refolding due to an enhanced protein solubility.
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- OSTI ID:
- 323783
- Journal Information:
- Biotechnology and Bioengineering, Vol. 62, Issue 6; Other Information: PBD: 20 Mar 1999
- Country of Publication:
- United States
- Language:
- English
Similar Records
A comparative study on the aggregating effects of guanidine thiocyanate, guanidine hydrochloride and urea on lysozyme aggregation
Precision measurements of binary and multicomponent diffusion coefficients in protein solutions relevant to crystal growth: Lysozyme chloride in water and aqueous NaCl at pH 4.5 and 25{degree}C
Protein-salt binding data from potentiometric titrations of lysozyme in aqueous solutions containing KCl
Journal Article
·
Fri Aug 08 00:00:00 EDT 2014
· Biochemical and Biophysical Research Communications
·
OSTI ID:323783
Precision measurements of binary and multicomponent diffusion coefficients in protein solutions relevant to crystal growth: Lysozyme chloride in water and aqueous NaCl at pH 4.5 and 25{degree}C
Journal Article
·
Wed Apr 14 00:00:00 EDT 1999
· Journal of the American Chemical Society
·
OSTI ID:323783
+2 more
Protein-salt binding data from potentiometric titrations of lysozyme in aqueous solutions containing KCl
Technical Report
·
Sat Mar 01 00:00:00 EST 1997
·
OSTI ID:323783