VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Isolation and properties of myeloperoxidase from human bone marrow

   
Shafran M.G.
PubMed Id: 220800
Year: 1979  Volume: 25  Issue: 2  Pages: 149-153
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.
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Shafran, M. G. (1979). Isolation and properties of myeloperoxidase from human bone marrow. Voprosy Meditsinskoi Khimii, 25(2), 149-153.
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