Lysozyme Ch was hydrolyzed with trypsin in 2 M urea and the resulting peptides were separated by a combination of gel filtration and ion exchange chromatography. Ten peptides and free lysine were produced by tryptic action. The enzyme has 5 arginine and 4 lysine residues per molecule and one of the peptides arose from a chymotryptic-like cleavage of a tyrosyl-seryl bond near the amino-terminal end of the enzyme. The entire molecule is accounted for by the tryptic peptides, which have been ordered withing the peptides obtained by cyanogen bromide cleavage of the molecule.
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Wahba et al. (1975) studied this question.