Abstract
Using a concanavalin A high-performance liquid affinity chromatography system, the effect of slow solute desorption from the silica-bound ligand on protein recovery and peak shape has been investigated. The desorption of glycoproteins from the immobilized concanavalin A was found to be many times slower than the desorption of monovalent carbohydrates. To overcome the kinetic limitations of this chromatographic system, a novel method of protein elution, stopped-flow elution, was developed and used to ovalbumin and to examine the kinetic "sluggishness" of the desorption process. The stopped-flow elution method allows the quantitative recovery of purified glycoprotein in a volume of approximately 0.5 ml.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 235-246 |
| Number of pages | 12 |
| Journal | Journal of Chromatography A |
| Volume | 294 |
| Issue number | C |
| DOIs | |
| State | Published - 1984 |
Bibliographical note
Funding Information:The authors gratefullya cknowledgeR . R. Walters for many helpful discus-sionsc oncerningt his work. Financial supportf or A. J. Muller was providedb y the National ScienceF oundation (CHE 8217363).