Isolation and properties of human neutrophil myeloperoxidase.
Isolation and properties of human neutrophil myeloperoxidase.
复制标题
人中性粒细胞髓过氧化物酶的分离和特性。
DOI:
10.1021/bi00505a015
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Travis,J
中科院分区:
文献类型:
--
作者:
Matheson,NR;Wong,PS;Travis,J
N. R. Matheson, PS Wong, and J. Travis* abstract: Human leukocyte myeloperoxidase has been pu-rified to homogeneity by a three-step procedure which includes dialysis of a granule extract against low-salt buffer, Sephadex G-75 chromatography, and carboxymethylcellulose chroma-tography. The final product was homogeneous when examined by acid polyacrylamide gel electrophoresis and sedimentation equilibrium ultracentrifugation. The molecular weight de-termined by the latter procedure was 118 000. With or without reduction of the protein by 2-mercaptoethanol, subunits were formed which migrated as a single band after sodiumdodecyl sulfate gel electrophoresis. With reduction, the molecular weight of the apparently identical subunits was 59 000, andDuring acute inflammation, polymorphonuclear leukocytes collect in large numbers by directed migration from the vas-cular space into the tissues. Within these cells are cytoplasmic granules containing oxidative and hydrolytic enzymes. Al-though the primary role of these enzymes is the destruction of microorganisms and debris within the phagocyte vacuole, it has become increasingly clear they also participate in ex-tracellular reactions.