[Isolation and some properties of mink lysozyme].

Lysozyme (EC 3.2.1.17) from spleen, kidney and liver of mink was isolated by affinity chromatography on deaminated chitin. The histidine content of mink lysozyme is unusually high and comprises 7 residues per mole of the protein. The acidic and basic amino acid residues are present in the mink lysozyme in nearly equal amounts (20-22); in this respect, the degree of amidation of the side chain carboxylic groups is relatively low (8-10). The lysozyme preparations obtained are found to contain an unknown, tightly bound component, absorbing at 400-420 nm.