Affinity chromatographic purification of human lysozyme, with special reference to human leukemia lysozyme.
Lysozyme [EC 3.2.1.17] was purified from human tears, serum, and urine of acute monocytic leukemia patients, renal disease patients, and residents in cadmium-polluted areas of Tsushima Island using an affinity adsorbent containing lysozyme-lysate of Micrococcus lysodeikticus cell walls as the ligand. By means of this procedure, leukemia lysozyme was purified 100- to 200-fold with an activity recovery of 80%. It was crystallized at pH 10. This purified preparation appeared homogeneous in disc electrophoresis and showed a specific activity 2.5-fold higher than that of crystalline lysozyme from hen egg-white. Tear lysozyme was also purified to a nearly homogeneous state while the enzymes from normal serum and urine of a nephrosis patient and of residents in cadmium-polluted area were still disc electrophoretically heterogeneous and showed low specific activity as compared with purified leukemia lysozyme.
D000596:Amino Acids / Q000032:analysis; D002846:Chromatography, Affinity; D003460:Crystallization; D006801:Humans; D007674:Kidney Diseases / Q000201:enzymology; D007948:Leukemia, Monocytic, Acute / Q000201:enzymology*; D009113:Muramidase / Q000302:isolation & purification / Q000378:metabolism; D013666:Tears / Q000201:enzymology
D000596:Amino Acids; D009113:Muramidase