[Isolation and some properties of mink lysozyme]. / Vydelenie i nekotorye s voistva lizotsima norka.

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.