[Isolation and properties of myeloperoxidase from human bone marrow]

A preparation of myeloperoxidase was isolated from human bone marrow by column chromatography on DEAE-Sephadex, CM cellulose and gel filtration on Sephadex G-100. The enzyme was purified to 0.76 purity with a 16% yield. The repeated gel filtration, E430/E280 ratio and immunochemical study confirm the high degree of purification. Molecular weight of the enzyme, determined by gel filtration on Sephadex G-100, was 150000.