Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family.
Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family.
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DOI：
10.1084/jem.169.5.1757
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发表时间：
1989-05-01
期刊：
影响因子：
--
通讯作者：
Gleich GJ
中科院分区：
文献类型：
--
作者：
Ten RM;Pease LR;McKean DJ;Bell MP;Gleich GJ
人嗜酸性粒细胞过氧化物酶（EPO）是从嗜酸性粒细胞增多症患者的外周血中提取的。通过凝胶过滤测定H和L亚基的分子量分别为57，000和11，000道尔顿。两个亚基的部分氨基酸序列用于构建寡核苷酸，用于筛选几个cDNA文库，包括来自人诱导的脐带单核细胞的cDNA文库。分离对应于EPO的cDNA克隆。核苷酸序列显示了2，106 bp的开放阅读框，依次对应于前序列、L链和H链。比较EPO的核苷酸序列与其他过氧化物酶，如髓过氧化物酶，表明存在一个多基因家族。
Human eosinophil peroxidase (EPO) was purified from eosinophil granules derived from the peripheral blood of patients with eosinophilia. The molecular mass of the H and L subunits was determined by gel filtration to be 57,000 and 11,000 daltons, respectively. The partial amino acid sequences of both subunits were used to construct oligonucleotides for the screening of several cDNA libraries, including one derived from human-induced umbilical cord mononuclear cells. A cDNA clone was isolated corresponding to EPO. The nucleotide sequence revealed an open reading frame of 2,106 bp, corresponding to a prosequence, L chain, and H chain, in this order. Comparison of the EPO nucleotide sequence with other peroxidases, such as myeloperoxidase, suggests the existence of a multigene family.