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鸡红细胞特异性主要组织相容性复合体抗原。利用单克隆抗体对B-G抗原进行表征与纯化。

The chicken erythrocyte-specific MHC antigen. Characterization and purification of the B-G antigen by monoclonal antibodies.

作者信息

Salomonsen J, Skjødt K, Crone M, Simonsen M

出版信息

Immunogenetics. 1987;25(6):373-82. doi: 10.1007/BF00396103.

Abstract

Mouse monoclonal antibodies with B-G antigen (major histocompatibility complex class IV) specificity were obtained after immunization with erythrocytes or partially purified B-G antigen. The specificities of the hybridoma antibodies were determined by precipitation of B-G antigens from 125I-labeled chicken erythrocyte membranes (CEM) followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and autoradiography. The B-G antigen had an approximate molecular mass of 46-48 kd in reduced samples, depending on the haplotype, and in unreduced samples contained either dimers (85 kd), when labeled erythrocytes were the antigen source, or trimers (130 kd), when B-G was purified and precipitated from CEM. The B-G antigen was unglycosylated as studied by in vitro synthesis in the presence or absence of tunicamycin, binding experiments with lectin from Phaseolus limensis, and treatment of purified B-G antigen with Endoglycosidase-F or trifluoromethanesulfonic acid. Two-way sequential immunoprecipitation studies of erythrocyte membrane extracts with anti-B-G alloantisera and monoclonal antibodies revealed only one population of B-G molecules. Pulse-chase experiments have shown B-G to be synthesized as a monomer, with dimerization taking place after 20-30 min. No change in the monomer's molecular mass due to posttranslational modifications was revealed. The antigen was purified from detergent extract of CEM by affinity chromatography with a monoclonal antibody, and then reduced and alkylated and affinity-purified once more. Finally, reverse-phase chromatography resulted in a pure product. The B-G antigen was identified in the various fractions by rocket immunoelectrophoresis. The final product was more than 99% pure, as estimated by SDS-PAGE analysis followed by silver stain of proteins. The yield from the affinity chromatography step was 3-4 micrograms B-G/ml blood, calculated from Coomassie-stained SDS-PAGE of B-G using ovalbumin standards. The monoclonal antibodies were also used to identify the B-G (class IV) precipitation arc in crossed immunoelectrophoresis. No common precipitate with the B-F (class I) antigen was observed.

摘要

用红细胞或部分纯化的B-G抗原(主要组织相容性复合体IV类)免疫后,获得了具有B-G抗原特异性的小鼠单克隆抗体。通过从125I标记的鸡红细胞膜(CEM)中沉淀B-G抗原,然后进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)和放射自显影,确定杂交瘤抗体的特异性。在还原样品中,B-G抗原的分子量约为46-48kd,这取决于单倍型;在未还原样品中,当标记红细胞为抗原来源时,含有二聚体(85kd),当从CEM中纯化并沉淀B-G时,含有三聚体(130kd)。通过在有无衣霉素存在下的体外合成、与利马豆凝集素的结合实验以及用内切糖苷酶-F或三氟甲磺酸处理纯化的B-G抗原,研究表明B-G抗原未糖基化。用抗B-G同种抗血清和单克隆抗体对红细胞膜提取物进行双向顺序免疫沉淀研究,结果显示只有一群B-G分子。脉冲追踪实验表明,B-G以单体形式合成,在20-30分钟后发生二聚化。未发现翻译后修饰导致单体分子量发生变化。用单克隆抗体通过亲和色谱从CEM的去污剂提取物中纯化抗原随后进行还原和烷基化,然后再次进行亲和纯化。最后,反相色谱得到纯产物。通过火箭免疫电泳在各个组分中鉴定出B-G抗原。根据蛋白质银染后的SDS-PAGE分析估计,最终产物的纯度超过99%。根据用卵清蛋白标准品对B-G进行考马斯亮蓝染色的SDS-PAGE计算,亲和色谱步骤的产量为3-4微克B-G/毫升血液。单克隆抗体还用于在交叉免疫电泳中鉴定B-G(IV类)沉淀弧。未观察到与B-F(I类)抗原的共同沉淀。

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