Hogarth P M, Walker I D, McKenzie I F, Springer T A
Proc Natl Acad Sci U S A. 1985 Jan;82(2):526-30. doi: 10.1073/pnas.82.2.526.
Serological and biochemical studies using monoclonal antibodies have demonstrated that the Ly-15 cell membrane alloantigens are polymorphic sites on the lymphocyte function-associated antigen-1 (LFA-1) molecule. Ly-15.2 and LFA-1 show identical tissue distributions, being present on all thymocytes, lymphocytes, and neutrophils, and flow cytofluorometric analysis indicated identical cell surface expression of these molecules. Identity of Ly-15.2 and LFA-1 was confirmed by immunochemical analysis. The Ly-15.2 and LFA-1 molecules have an identical heterodimeric structure of Mr 180,000 alpha chain and Mr 94,000 beta chain, which coelectrophorese on two-dimensional NaDodSO4/PAGE. Furthermore, anti-Ly-15.2 and anti-LFA-1 antibodies coprecipitate the same molecule from thymocyte lysates, and peptide mapping studies show that the Ly-15.2 and LFA-1 alpha chains are identical, as are the beta chains.
使用单克隆抗体进行的血清学和生化研究表明,Ly-15细胞膜同种异体抗原是淋巴细胞功能相关抗原-1(LFA-1)分子上的多态性位点。Ly-15.2和LFA-1显示出相同的组织分布,存在于所有胸腺细胞、淋巴细胞和中性粒细胞上,流式细胞荧光分析表明这些分子在细胞表面的表达相同。通过免疫化学分析证实了Ly-15.2和LFA-1的同一性。Ly-15.2和LFA-1分子具有相同的异二聚体结构,由分子量为180,000的α链和分子量为94,000的β链组成,它们在二维十二烷基硫酸钠/聚丙烯酰胺凝胶电泳(NaDodSO4/PAGE)中共电泳。此外,抗Ly-15.2和抗LFA-1抗体从胸腺细胞裂解物中共沉淀出相同的分子,肽图谱研究表明Ly-15.2和LFA-1的α链相同,β链也相同。