Papain-solubilized HL-A antigens from cultured human lymphocytes contain two peptide fragments.
Papain-solubilized HL-A antigens from cultured human lymphocytes contain two peptide fragments.
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来自培养的人淋巴细胞的木瓜蛋白酶溶解的 HL-A 抗原含有两个肽片段。
DOI：
10.1073/pnas.70.5.1603
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发表时间：
1973
影响因子：
11.1
通讯作者：
J. Strominger
中科院分区：
文献类型：
--
作者：
P. Cresswell;M. Turner;J. Strominger
用木瓜蛋白酶从培养的人淋巴细胞中溶解HL-A2和HL-A7抗原，并在形成免疫复合物后以小放射性规模纯化，或用柱层析方法大规模纯化。在这两种情况下，已经表明，所获得的材料由两个非共价结合的片段组成。一个片段是分子量为30，000 - 31，000的糖肽，另一个片段是分子量为11，000 - 12，000的肽。在含8 M尿素的聚丙烯酰胺凝胶中，HL-A2和HL-A7的大片段表现出不同的电泳迁移率，而小片段则相同。讨论了这些材料与天然HL-A分子的关系。
HL-A 2 and HL-A 7 antigens have been solubilized from cultured human lymphocytes by papain and purified on a small radioactive scale after formation of immune complexes, or on a large scale by column chromatographic methods. In both cases, it has been shown that the materials obtained consist of two noncovalently bound fragments. One fragment is a glycopeptide of molecular weight 30,000-31,000, the other is a peptide of molecular weight 11,000-12,000. In polyacrylamide gels containing 8 M urea, the large fragments of HL-A 2 and HL-A 7 exhibited different electrophoretic mobilities, while the small fragments were the same. The relationship of these materials to the native HL-A molecule is discussed.