Abstract
Lysozymes from animal and plant sources have been purified on agarose derivatives containing a phenylacetyl ligand. While this adsorbent can also bind chymotrypsin, the use of imidazole permits separation of lysozymes from the protease. The phenylacetyl-agarose is a general affinity sorbent bearing a ligand of non-biochemical origin in contrast to those, for example, which use nucleotide cofactors. By careful selection of desorption conditions, different enzymes can be purified with the same sorbent. Results also suggest that binding of lysozymes to an affinity ligand does not require a leash structure between ligand and support matrix.