ISSN:
1573-4943
Keywords:
protein stabilization by salts
;
free energy of stabilization
;
protein denaturation by guanidine hydrochloride
;
lyotropic salt effects on proteins
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The denaturation of proteins by guanidine hydrochloride was studied in the presence of different concentrations of stabilizing salts, namely potassium phosphate, ammonium sulfate, and potassium acetate. The denaturation transition was followed by observing changes in the peptide circular dichroism atpH 7.0 and 25°C. From these results the free energy of stabilization for the process native ⇄ denatured was determined. It was found that the stabilizing power of the anions increased in the order acetate 〈 sulfate 〈 phosphate, in agreement with the anionic lyotropic series. Ribonuclease A, which is known to have a site that can bind either a phosphate or a sulfate ion, showed a larger stabilization by these anions than that for lysozyme, pepsinogen, and myoglobin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01025963
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