Cation-exchange displacement chromatography of proteins with protamine displacers: effect of induced salt gradients.
Protamine was investigated for its utility as a protein displacer in cation-exchange systems. Although the protamine solution contained several variants of the molecule, the high affinity of all of the components in this heterogeneous biopolymer enabled it to act as an efficient protein displacer. To facilitate parameter estimation of the protamine, a preliminary purification was carried out by preparative elution chromatography. Chromatographic parameters of both the feed proteins and protamine displacer were obtained for use in a multicomponent steric mass action ion-exchange displacement model. Model simulations were compared to displacement results under both moderate and intense induced salt gradient conditions. In both cases, excellent agreement was obtained between the displacement experiments and theoretical predictions. In addition, these studies serve to dramatize the importance of induced salt gradients in ion-exchange displacement systems.
Isermann Department of Chemical Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180-3590.
J A
JA
Gerstner
S M
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Cramer
D000595:Amino Acid Sequence; D000818:Animals; D001709:Biotechnology; D002852:Chromatography, Ion Exchange / Q000379:methods*; D005069:Evaluation Studies as Topic; D008969:Molecular Sequence Data; D011479:Protamines / Q000737:chemistry / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification*; D012492:Salts
D011479:Protamines; D011506:Proteins; D012492:Salts