[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.
D001853:Bone Marrow / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D008970:Molecular Weight; D009195:Peroxidase / Q000032:analysis / Q000302:isolation & purification*; D010544:Peroxidases / Q000302:isolation & purification*; D013057:Spectrum Analysis
D010544:Peroxidases; D009195:Peroxidase
Vydelenie i nekotorye svoĭstva mieloperoksidazy kostnogo mozga cheloveka.