Contribution of ionically immobilized bovine serum albumin to the retention of enantiomers.
The retention of the enantiomers of mandelic acid and N-benzoylalanine was studied on columns prepared by immobilizing bovine serum albumin (BSA) on an anion exchanger. The amount of BSA fixed on the column is easy to adjust and measure. The adsorption isotherms were determined. For each enantiomer, the isotherm is well accounted for by a bi-Langmuir equation. One term of the isotherm (which is the same for both enantiomers) corresponds to non-selective interactions and the other term to the chiral selective interactions. The column saturation capacity of this second term is 8% larger for the less strongly retained enantiomer. This saturation capacity corresponds approximately to one enantiomer molecule adsorbed for five BSA molecules immobilized. This result is in agreement with the assumption of the hydrophobic cavity of BSA being the chiral selective site.
Jacobson
S C
SC
Department of Chemistry, University of Tennessee, Knoxville 37996-1501.
Guiochon
G
G
D000409:Alanine / Q000031:analogs & derivatives / Q000032:analysis; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange / Q000379:methods*; D008333:Mandelic Acids / Q000032:analysis; D012710:Serum Albumin, Bovine; D013237:Stereoisomerism
D008333:Mandelic Acids; C047207:N-benzoylalanine; D012710:Serum Albumin, Bovine; D000409:Alanine