Isolation and properties of human neutrophil myeloperoxidase.

Isolation and properties of human neutrophil myeloperoxidase.
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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
Travis,J
中科院分区:
生物学3区
文献类型:
--
作者:
Matheson,NR;Wong,PS;Travis,J

文献摘要

被引文献

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摘要:人白细胞髓过氧化物酶的纯化采用三步法,包括低盐缓冲液透析、Sephadex G-75柱层析和羧甲基纤维素层析。经酸性聚丙烯酰胺凝胶电泳法和沉淀平衡超速离心法鉴定,最终产物均一。后一种方法测得的相对分子质量为118 000。在用2-巯基乙醇还原或不还原蛋白质的情况下,形成亚基,经十二烷基硫酸钠凝胶电泳后,亚基以单一条带的形式迁移。减少后,明显相同的亚基的分子量为59000,在急性炎症时,中性粒细胞从血管间隙定向迁移到组织中,聚集了大量的中性粒细胞。在这些细胞内是含有氧化酶和水解酶的细胞质颗粒。虽然这些酶的主要作用是破坏吞噬细胞液泡内的微生物和碎片,但越来越明显的是,它们也参与细胞外的反应。
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.