Abstract
The release of immobilized ligands from cellulose beads was studied by solvolytic detachment of glycine, dl-leucine, azocasein and leucine aminopeptidase, which were coupled to carbonochloridate-activated supports. It is demonstrated with immobilized glycine and leucine that the urethane linkage formed between the matrix and ligands is very stable in the pH range 2–10. Comparison of the leakage with corresponding Sepharose conjugates shows the superiority of conjugates based on cellulose beads. The release of immobilized amino acids from bead cellulose was less than 1% for 1000 h at room temperature. For the immobilized proteins it is shown that the initial leakage is due to the desorption of a small amount of non-covalently bound protein (< 10%). Leakage of the proteins multivalently bound to the matrix by the urethane bond was not detectable.
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