Chersi A, Houghten R A, Morganti M C, Muratti E
Regina Elena Institute for Cancer Research, Rome, Italy.
Z Naturforsch C J Biosci. 1987 Nov-Dec;42(11-12):1313-8. doi: 10.1515/znc-1987-11-1227.
Repeated immunizations of rabbits with chemically synthesized peptides from selected regions of HLA-DP histocompatibility antigens resulted in the production of specific antibodies that were then isolated from the immune sera by chromatography on Sepharose-peptide immunoadsorbents. The purified antibodies, when tested with an enzyme-linked immunosorbent assay, specifically bound to the inciting fragments; moreover, two of them recognized glycoproteins extracted by nonionic detergents from human chronic lymphocytic leukemia cells, as revealed by binding assays. The results suggest that amino acid stretches 51-61 of the alpha chain and 80-90 of the beta chain of HLA-DP histocompatibility antigens are likely exposed on the surface of the protein molecule. The specific recognition of DP regions is strongly suggested by the difference in the binding of those antibodies to soluble membrane proteins, as compared to the binding of monomorphic anti-Class II monoclonal antibodies to the same antigens.
用来自HLA - DP组织相容性抗原选定区域的化学合成肽对兔子进行反复免疫，可产生特异性抗体，然后通过在琼脂糖 - 肽免疫吸附剂上进行层析从免疫血清中分离出这些抗体。用酶联免疫吸附测定法检测时，纯化后的抗体与引发片段特异性结合；此外，结合试验表明，其中两种抗体识别从人慢性淋巴细胞白血病细胞中用非离子去污剂提取的糖蛋白。结果表明，HLA - DP组织相容性抗原α链的51 - 61氨基酸片段和β链的80 - 90氨基酸片段可能暴露在蛋白质分子表面。与单态抗II类单克隆抗体对相同抗原的结合相比，这些抗体与可溶性膜蛋白结合的差异强烈表明对DP区域具有特异性识别。
