Structure, assembly, conformation, and immunological properties of the two subunit classes of ferritin.
Structure, assembly, conformation, and immunological properties of the two subunit classes of ferritin.
复制标题
铁蛋白两个亚基类别的结构、组装、构象和免疫学特性。
DOI：
10.1021/bi00521a020
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Listowsky,I
中科院分区：
文献类型：
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作者：
Otsuka,S;Maruyama,H;Listowsky,I
Shinobu Otsuka，1 Hiroshi Maruyama，and欧文Listowsky* 摘要：人肝铁蛋白的两种亚基类型被纯化至均一。这两个亚基以明确的方式重新组装，并形成球形颗粒，在电子显微镜下重新组装天然脱铁铁蛋白。亲和层析方法，以获得专门与H或与L多肽相互作用的抗体的制剂，表明不同的免疫学特性可以归因于铁蛋白的每个亚基。亚基的氨基酸组成相似，但较大的H亚基具有较少的亮氨酸，苯丙氨酸和精氨酸残基。因此，H亚基不可能经历蛋白水解加工，并且是L亚基的前体。圆二色谱数据表明，HOM-
Shinobu Otsuka, 1 Hiroshi Maruyama, and Irving Listowsky* abstract: The two subunit types of human liver ferritin were purified to homogeneity. Both subunits reassembled in a well-defined manner and formed spherical particles that re-sembled natural apoferritin in electron micrographs. Affinity chromatography methods were employed to obtain preparations of antibodies that interacted exclusively either with the H or with the L polypeptides, demonstrating that distinct immunological properties may be ascribed to each subunit of ferritin. The amino acid compositions of the subunits were similar, but the larger H subunit had fewer leucine, phenyl-alanine, and arginine residues. It is therefore improbable that H subunits undergo proteolytic processing and are precursors for L subunits. Circular dichroism data indicated that hom-