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Purification of lysozyme from other hen's‐egg‐white proteins using metal‐affinity precipitation

It was found that the presence of 5 mM Cu2+ caused precipitation of protein present in hen's egg white to a large extent. About 85% of lysozyme activity remained in the supernatant and the enzyme was purified by approx. 13‐fold. A further gel‐filtration step on Sephadex G‐75 resulted in an overall yield of 80% for the enzyme with 655‐fold purification, and showed a single band on SDS/PAGE.