ISSN:
1612-1112
Keywords:
Column liquid chromatography
;
Preparative scale separations
;
Strong cation-exchange resin
;
Amino acids
;
Desalting
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary The uptake of sodium chloride, leucine and phenylalanine by a strong cation-exchange resin in the sodium form have been compared. Sodium chloride was excluded from the resin, as indicated by its parabolic upwards curved isotherm, and the corresponding desorption edge was sharpened (constant pattern). Isotherms for both amino acids constructed from a single elution experiment displayed slightly downwards curvature; the corresponding desorption edges spread in contrast to the breakthrough ones. The affinities of both amino acids for the resin were higher (from 15 to 40 %) in the presence of 1 M sodium chloride, indicating that hydrophobic interactions played a significant role in the mechanism of sorption. As expected from the isotherms, a mixture of 1 M sodium chloride, leucine and phenylalanine was separated with satisfactory recovery of both amino acids for a column loading of 10 % of the bed volume. Real mother liquors have also been separated under the same conditions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02466388
Permalink
