通过异种多克隆和单克隆抗血清鉴定的人β2-微球蛋白上的表位位点。
Epitope sites on human beta 2-microglobulin identified by xenogeneic polyclonal and monoclonal antisera.
作者信息
Sanderson A R, Ward P J
出版信息
Immunology. 1981 Sep;44(1):169-75.
The relationship between the ability to produce insoluble antigen--antibody complexes from a polypeptide antigen, beta 2-microglobulin and specific antisera from several different species has been examined. The size of complexes was determined by gel-filtration chromatography using serum, immunoglobulin, and divalent F(ab')2 or monovalent Fab fragments therefrom. Non-precipitating primate antihuman beta 2-microglobulin sera recognized two epitopes on the antigen and monoclonal antibody only one epitope, whereas precipitating antisera recognized three or more epitopes, as lattice theory predicts. The paucity of epitope sites reaffirms the unusual immunogenicity of human beta 2-microglobulin when presented to certain primates in the form of an HLA antigen.
已对从一种多肽抗原、β2微球蛋白以及来自几种不同物种的特异性抗血清产生不溶性抗原-抗体复合物的能力之间的关系进行了研究。使用血清、免疫球蛋白以及由此产生的二价F(ab')2或单价Fab片段，通过凝胶过滤色谱法测定复合物的大小。非沉淀性灵长类抗人β2微球蛋白血清识别抗原上的两个表位，而单克隆抗体仅识别一个表位，而沉淀性抗血清识别三个或更多表位，正如晶格理论所预测的那样。表位位点的稀少再次证实了人β2微球蛋白以HLA抗原形式呈现给某些灵长类动物时具有不同寻常的免疫原性。
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