Blackledge G, Vose B, Morris A J, Crowther D, Gallagher J T
Biochem J. 1982 Oct 15;208(1):69-75. doi: 10.1042/bj2080069.
The binding of fluorescein-conjugated lentil lectin and concanavalin A to the surface membrane of human peripheral blood lymphocytes was studied by flow cytometry. The lymphocytes bound 3-fold more lentil lectin molecules compared with concanavalin A molecules and lentil lectin binding approached saturation at a much lower concentration than did that of concanavalin A. Lentil lectin identified two groups of lymphocytes: a low-binding T-cell fraction and a high-binding B-cell-enriched fraction. Concanavalin A did not discriminate between these populations in unseparated lymphocytes. Competition studies indicated that lentil lectin and concanavalin A were bound to different sites on the lymphocyte surface, although about 50% of lentil lectin sites were in close proximity to concanavalin A sites.
通过流式细胞术研究了荧光素偶联的扁豆凝集素和伴刀豆球蛋白A与人外周血淋巴细胞表面膜的结合。与伴刀豆球蛋白A分子相比,淋巴细胞结合的扁豆凝集素分子多3倍,且扁豆凝集素结合在比伴刀豆球蛋白A低得多的浓度下接近饱和。扁豆凝集素识别出两组淋巴细胞:低结合T细胞部分和高结合富含B细胞的部分。在未分离的淋巴细胞中,伴刀豆球蛋白A不能区分这些群体。竞争研究表明,扁豆凝集素和伴刀豆球蛋白A结合在淋巴细胞表面的不同位点,尽管约50%的扁豆凝集素位点与伴刀豆球蛋白A位点紧密相邻。