Chemical properties of two antigens controlled by the major histocompatibility complex of the chicken.
Chemical properties of two antigens controlled by the major histocompatibility complex of the chicken.
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由鸡的主要组织相容性复合体控制的两种抗原的化学特性。
DOI：
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发表时间：
1976
影响因子：
4.8
通讯作者：
R. Pink
中科院分区：
文献类型：
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作者：
A. Ziegler;R. Pink
研究了鸡主要组织相容性复合体控制的抗原化学。五个鸡株的外周血白细胞的放射性标记掺入氚化氨基酸，酶碘化，或温和的高碘酸氧化，然后用氚化硼氢化钠还原。用Nonidet P-40溶解膜结合抗原，并通过两步免疫沉淀法纯化。在还原或非还原条件下，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析所得免疫沉淀物。鸡主要组织相容性抗原（B抗原）由分子量（还原形式）为40，000至43，000和11，000至12，000的多肽链组成，根据其在内部校准凝胶中的迁移率推断。当从不同的鸡品系中分离时，较大的链在这种凝胶中可以具有略微不同的迁移率;因此，来自品系WA和WB的大多肽的迁移率分别对应于40，000和43，000的分子量。在非还原条件下运行的凝胶得到类似的结果;特别是没有检测到较大链的二聚体或寡聚体，因此排除了B抗原的免疫球蛋白样结构。大的链被高碘酸氧化还原过程标记，表明它们是糖蛋白（可能含有唾液酸），而小的多肽不能被这种方法标记。一种特殊的抗B血清可从~ 3 H-氨基酸标记的白细胞裂解物中沉淀出表观分子量约为30，000的一种或多种蛋白质。这种蛋白质，命名为B-L，与B主要组织相容性抗原的不同之处在于它不与分子量为11，000至12，000的小链相关，并且不存在于红细胞上。因此，鸡主要组织相容性复合体中至少有两条蛋白质链由基因编码（或由基因控制其合成）。
The chemistry of antigens controlled by the major histocompatibility complex of the chicken has been investigated. Peripheral blood leukocytes of five chicken strains were radioactively labeled by incorporation of tritiated amino acids, enzymatic iodination, or mild periodate oxidation followed by reduction with tritiated sodium borohydride. Membrane-bound antigens were solubilized with Nonidet P-40 and purified by a two-step immunoprecipitation procedure. The resulting immunoprecipitates were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing or nonreducing conditions. The chicken major histocompatibility antigens (B antigens) are composed of polypeptide chains with molecular weights (in the reduced form) of 40,000 to 43,000 and 11,000 to 12,000, as deduced from their mobilities in internally calibrated gels. The larger chains, when isolated from different chicken strains, can have slightly different mobilities in such gels; thus the mobilities of the large polypeptides from strains WA and WB correspond to molecular weights of 40,000 and 43,000, respectively. Gels run under nonreducing conditions give similar results; in particular no dimers or oligomers of the larger chains are detectable, thus ruling out an immunoglobulin-like structure for the B antigens. The large chains are labeled by the periodate oxidation-reduction procedure, suggesting that they are glycoproteins (probably containing sialic acid), while the small polypeptides cannot be labeled by this method. An additional protein or proteins of apparent molecular weight about 30,000 could be precipitated from 3H-amino-acid-labeled leukocyte lysates by one particular anti-B serum. This protein(s), named B-L, differs from the B major histocompatibility antigens in that it is not associated with the small chain of molecular weight 11,000 to 12,000 and does not occur on erythrocytes. Thus, at least two protein chains are coded for (or have their synthesis controlled by) genes in the chicken major histocompatibility complex.