[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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D006639:Histidine / Q000032:analysis; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008907:Mink; D009113:Muramidase / Q000302:isolation & purification*; D013154:Spleen / Q000201:enzymology*
D000596:Amino Acids; D006639:Histidine; D009113:Muramidase
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