The monoclonal antibody, UCHL1, recognizes a 180,000 MW component of the human leucocyte-common antigen, CD45.
The monoclonal antibody, UCHL1, recognizes a 180,000 MW component of the human leucocyte-common antigen, CD45.
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单克隆抗体 UCHL1 可识别人类白细胞共同抗原 CD45 的 180,000 MW 成分。
作者：
L. Terry;M. Brown;P.C.L. Beverley
白细胞共同抗原（L-CA或CD 45）是一个高分子量糖蛋白家族，分子量范围为180，000至220，000 MW，仅在淋巴和骨髓来源的细胞上表达。CD 45单克隆抗体（mAb）识别存在于该家族的所有多肽上的表位，而称为CD 45 R的其它mAb识别仅在220，000 MW和200，000 MW多肽上发现的决定簇。相比之下，mAb UCHL 1识别180，000 MW抗原。使用UCHL 1偶联的琼脂糖凝胶珠从细胞系的裂解物中吸收抗原。CD 45 mAb结合于该固定的抗原。用CD 45 mAb偶联的琼脂糖凝胶珠固定的抗原结合UCHL 1。通过用CD 45 mAb偶联的珠从MOLT-4细胞系吸收和洗脱纯化的抗原产生180，000和190，000 MW的分子。用UCHL 1再沉淀洗脱的抗原，仅产生180，000 MW条带。在一个相反的实验中，CD 45 mAb从纯化的UCHL 1抗原中再沉淀180，000 MW分子。UCHL 1和CD 45 R mAb 2 H4显示出与人T细胞和B细胞系的相互排斥的反应模式，但在两个髓系和一个红白血病细胞系上观察到抗原的共表达。与此相反，其他推定的CD 45 R单克隆抗体识别的表位与UCHL 1共表达的髓系，红系和许多T-和B-细胞系。我们得出结论，UCHL 1识别仅存在于CD 45的180，000 MW多肽上的表位。该抗原的表达基本上与CD 45 R mAb 2 H4检测到的表位相反。
The leucocyte-common antigen (L-CA or CD45) is a family of high molecular weight glycoproteins, ranging from 180,000 to 220,000 MW that are expressed only on cells of lymphoid and myeloid origin. CD45 monoclonal antibodies (mAbs) recognize epitopes present on all polypeptides of the family, while other mAbs, termed CD45R, recognize determinants found only on the 220,000 MW and 200,000 MW polypeptides. In contrast the mAb UCHL1 recognizes a 180,000 MW antigen. UCHL1-coupled Sepharose beads were used to absorb antigen from lysates of cell lines. CD45 mAbs bound to this immobilized antigen. Antigen immobilized with CD45 mAb-coupled Sepharose beads bound UCHL1. Antigen purified by absorption and elution from the MOLT-4 cell line with CD45 mAb-coupled beads yielded molecules of 180,000 and 190,000 MW. Reprecipitation of the eluted antigen with UCHL1 resulted in a 180,000 MW band only. In a reciprocal experiment, CD45 mAb reprecipitated a 180,000 MW molecule from purified UCHL1 antigen. UCHL1 and the CD45R mAb 2H4 showed a mutually exclusive pattern of reactivity with human T- and B-cell lines, but co-expression of the antigens was seen on two myeloid and one erythroleukaemic cell line. In contrast, epitopes recognized by other putative CD45R mAbs were co-expressed with UCHL1 both on myeloid, erythroid and many T- and B-cell lines. We conclude that UCHL1 recognizes an epitope present only on the 180,000 MW polypeptide of CD45. Expression of this antigen is essentially reciprocal to the epitope detected by the CD45R mAb 2H4.